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Benildo Sousa Cavada - One of the best experts on this subject based on the ideXlab platform.
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cdna cloning and 1 75 a crystal structure determination of ppl2 an endochitinase and n acetylglucosamine binding hemagglutinin from parkia Platycephala seeds
FEBS Journal, 2006Co-Authors: Benildo Sousa Cavada, Frederico Bruno Mendes Batista Moreno, Bruno A.m. Rocha, Walter Filgueira De Azevedo, Rolando E. R. Castellón, Georg V. Goersch, Celso Shiniti Nagano, Emmanuel P. Souza, Kyria S. Nascimento, Gandhi RadisbaptistaAbstract:Parkia Platycephala lectin 2 was purified from Parkia Platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia Platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407+/-15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia Platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia Platycephala lectin 2 hydrolyzed beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-length amino acid sequence of Parkia Platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 A resolution, showed that Parkia Platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (betaalpha)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.
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cDNA cloning and 1.75 Å crystal structure determination of PPL2, an endochitinase and N‐acetylglucosamine‐binding hemagglutinin from Parkia Platycephala seeds
The FEBS journal, 2006Co-Authors: Benildo Sousa Cavada, Frederico Bruno Mendes Batista Moreno, Bruno A.m. Rocha, Walter Filgueira De Azevedo, Rolando E. R. Castellón, Georg V. Goersch, Celso Shiniti Nagano, Emmanuel P. Souza, Kyria S. Nascimento, Gandhi Rádis-baptistaAbstract:Parkia Platycephala lectin 2 was purified from Parkia Platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia Platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407+/-15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia Platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia Platycephala lectin 2 hydrolyzed beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-length amino acid sequence of Parkia Platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 A resolution, showed that Parkia Platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (betaalpha)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.
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The First Crystal Structure of a Mimosoideae Lectin Reveals a Novel Quaternary Arrangement of a Widespread Domain
Journal of Molecular Biology, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Juan J. CalveteAbstract:The crystal structures of the apo and mannose-bound Parkia Platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of β-prism domains, and highlight the adaptability of the β-prism fold as a building block in the evolution of plant lectins. The P. Platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P. Platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P. Platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms.
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Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia Platycephala seeds.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Benildo Sousa Cavada, Bruno A.m. Rocha, Rolando E. R. Castellón, Celso Shiniti Nagano, Georg G. Vasconcelos, Gustavo Arruda Bezerra, Henri Debray, Plínio Delatorre, Marcos H. Toyama, Vicente De Paulo Teixeira PintoAbstract:A chitin-binding protein named PPL-2 was purified from Parkia Platycephala seeds and crystallized. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 55.19, b = 59.95, c = 76.60 A, and grew over several days at 293 K using the hanging-drop method. Using synchrotron radiation, a complete structural data set was collected to 1.73 A resolution. The preliminary crystal structure of PPL-2, determined by molecular replacement, presents a correlation coefficient of 0.558 and an R factor of 0.439. Crystallographic refinement is in progress.
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Energetics of 5-bromo-4-chloro-3-indolyl-α-d-mannose binding to the Parkia Platycephala seed lectin and its use for MAD phasing
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Javier Gómez, Sylviane Hoos, Patrick England, Juan J. CalveteAbstract:Parkia Platycephala belongs to the most primitive group of Leguminosae plants. Its seed lectin is made up of three homologous β-prism repeats and exhibits binding specificity for mannose/glucose. The properties of the association between the lectin from P. Platycephala seeds and monosaccharide ligands were analysed by isothermal titration calorimetry and surface plasmon resonance. The results are consistent with the lectin bearing three thermodynamically identical binding sites for mannose/glucose per monomer with dissociation constants in the millimolar range. Binding of each ligand by the lectin is enthalpically driven. Crystals have been obtained of the lectin in complex with a brominated derivative of mannose (5-bromo-4-chloro-3-indolyl-α-d-mannose), which were suitable for deriving an electron-density map by MAD phasing. In agreement with the thermodynamic data, six Br atoms were found in the asymmetric unit of the monoclinic P21 crystals, which contained two P. Platycephala lectin molecules. The availability of other Br derivatives of monosaccharides (glucose, galactose, fucose) may make this strategy widely useful for structure elucidation of novel lectins or when (as in the case of the P. Platycephala lectin) molecular-replacement methods fail.
Celso Shiniti Nagano - One of the best experts on this subject based on the ideXlab platform.
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cdna cloning and 1 75 a crystal structure determination of ppl2 an endochitinase and n acetylglucosamine binding hemagglutinin from parkia Platycephala seeds
FEBS Journal, 2006Co-Authors: Benildo Sousa Cavada, Frederico Bruno Mendes Batista Moreno, Bruno A.m. Rocha, Walter Filgueira De Azevedo, Rolando E. R. Castellón, Georg V. Goersch, Celso Shiniti Nagano, Emmanuel P. Souza, Kyria S. Nascimento, Gandhi RadisbaptistaAbstract:Parkia Platycephala lectin 2 was purified from Parkia Platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia Platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407+/-15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia Platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia Platycephala lectin 2 hydrolyzed beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-length amino acid sequence of Parkia Platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 A resolution, showed that Parkia Platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (betaalpha)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.
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cDNA cloning and 1.75 Å crystal structure determination of PPL2, an endochitinase and N‐acetylglucosamine‐binding hemagglutinin from Parkia Platycephala seeds
The FEBS journal, 2006Co-Authors: Benildo Sousa Cavada, Frederico Bruno Mendes Batista Moreno, Bruno A.m. Rocha, Walter Filgueira De Azevedo, Rolando E. R. Castellón, Georg V. Goersch, Celso Shiniti Nagano, Emmanuel P. Souza, Kyria S. Nascimento, Gandhi Rádis-baptistaAbstract:Parkia Platycephala lectin 2 was purified from Parkia Platycephala (Leguminosae, Mimosoideae) seeds by affinity chromatography and RP-HPLC. Equilibrium sedimentation and MS showed that Parkia Platycephala lectin 2 is a nonglycosylated monomeric protein of molecular mass 29 407+/-15 Da, which contains six cysteine residues engaged in the formation of three intramolecular disulfide bonds. Parkia Platycephala lectin 2 agglutinated rabbit erythrocytes, and this activity was specifically inhibited by N-acetylglucosamine. In addition, Parkia Platycephala lectin 2 hydrolyzed beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin. The full-length amino acid sequence of Parkia Platycephala lectin 2, determined by N-terminal sequencing and cDNA cloning, and its three-dimensional structure, established by X-ray crystallography at 1.75 A resolution, showed that Parkia Platycephala lectin 2 is homologous to endochitinases of the glycosyl hydrolase family 18, which share the (betaalpha)8 barrel topology harboring the catalytic residues Asp125, Glu127, and Tyr182.
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The First Crystal Structure of a Mimosoideae Lectin Reveals a Novel Quaternary Arrangement of a Widespread Domain
Journal of Molecular Biology, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Juan J. CalveteAbstract:The crystal structures of the apo and mannose-bound Parkia Platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of β-prism domains, and highlight the adaptability of the β-prism fold as a building block in the evolution of plant lectins. The P. Platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P. Platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P. Platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms.
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Crystallization and preliminary X-ray diffraction analysis of a new chitin-binding protein from Parkia Platycephala seeds.
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Benildo Sousa Cavada, Bruno A.m. Rocha, Rolando E. R. Castellón, Celso Shiniti Nagano, Georg G. Vasconcelos, Gustavo Arruda Bezerra, Henri Debray, Plínio Delatorre, Marcos H. Toyama, Vicente De Paulo Teixeira PintoAbstract:A chitin-binding protein named PPL-2 was purified from Parkia Platycephala seeds and crystallized. Crystals belong to the orthorhombic space group P212121, with unit-cell parameters a = 55.19, b = 59.95, c = 76.60 A, and grew over several days at 293 K using the hanging-drop method. Using synchrotron radiation, a complete structural data set was collected to 1.73 A resolution. The preliminary crystal structure of PPL-2, determined by molecular replacement, presents a correlation coefficient of 0.558 and an R factor of 0.439. Crystallographic refinement is in progress.
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Energetics of 5-bromo-4-chloro-3-indolyl-α-d-mannose binding to the Parkia Platycephala seed lectin and its use for MAD phasing
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Javier Gómez, Sylviane Hoos, Patrick England, Juan J. CalveteAbstract:Parkia Platycephala belongs to the most primitive group of Leguminosae plants. Its seed lectin is made up of three homologous β-prism repeats and exhibits binding specificity for mannose/glucose. The properties of the association between the lectin from P. Platycephala seeds and monosaccharide ligands were analysed by isothermal titration calorimetry and surface plasmon resonance. The results are consistent with the lectin bearing three thermodynamically identical binding sites for mannose/glucose per monomer with dissociation constants in the millimolar range. Binding of each ligand by the lectin is enthalpically driven. Crystals have been obtained of the lectin in complex with a brominated derivative of mannose (5-bromo-4-chloro-3-indolyl-α-d-mannose), which were suitable for deriving an electron-density map by MAD phasing. In agreement with the thermodynamic data, six Br atoms were found in the asymmetric unit of the monoclinic P21 crystals, which contained two P. Platycephala lectin molecules. The availability of other Br derivatives of monosaccharides (glucose, galactose, fucose) may make this strategy widely useful for structure elucidation of novel lectins or when (as in the case of the P. Platycephala lectin) molecular-replacement methods fail.
Juan J. Calvete - One of the best experts on this subject based on the ideXlab platform.
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The First Crystal Structure of a Mimosoideae Lectin Reveals a Novel Quaternary Arrangement of a Widespread Domain
Journal of Molecular Biology, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Juan J. CalveteAbstract:The crystal structures of the apo and mannose-bound Parkia Platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of β-prism domains, and highlight the adaptability of the β-prism fold as a building block in the evolution of plant lectins. The P. Platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P. Platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P. Platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms.
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Energetics of 5-bromo-4-chloro-3-indolyl-α-d-mannose binding to the Parkia Platycephala seed lectin and its use for MAD phasing
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Javier Gómez, Sylviane Hoos, Patrick England, Juan J. CalveteAbstract:Parkia Platycephala belongs to the most primitive group of Leguminosae plants. Its seed lectin is made up of three homologous β-prism repeats and exhibits binding specificity for mannose/glucose. The properties of the association between the lectin from P. Platycephala seeds and monosaccharide ligands were analysed by isothermal titration calorimetry and surface plasmon resonance. The results are consistent with the lectin bearing three thermodynamically identical binding sites for mannose/glucose per monomer with dissociation constants in the millimolar range. Binding of each ligand by the lectin is enthalpically driven. Crystals have been obtained of the lectin in complex with a brominated derivative of mannose (5-bromo-4-chloro-3-indolyl-α-d-mannose), which were suitable for deriving an electron-density map by MAD phasing. In agreement with the thermodynamic data, six Br atoms were found in the asymmetric unit of the monoclinic P21 crystals, which contained two P. Platycephala lectin molecules. The availability of other Br derivatives of monosaccharides (glucose, galactose, fucose) may make this strategy widely useful for structure elucidation of novel lectins or when (as in the case of the P. Platycephala lectin) molecular-replacement methods fail.
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Energetics of 5-bromo-4-chloro-3-indolyl-alpha-D-mannose binding to the Parkia Platycephala seed lectin and its use for MAD phasing.
Acta crystallographica. Section F Structural biology and crystallization communications, 2005Co-Authors: Francisca Gallego Del Sol, Javier Gómez, Sylviane Hoos, Patrick England, Celso S Nagano, Benildo S Cavada, Juan J. CalveteAbstract:Parkia Platycephala belongs to the most primitive group of Leguminosae plants. Its seed lectin is made up of three homologous beta-prism repeats and exhibits binding specificity for mannose/glucose. The properties of the association between the lectin from P. Platycephala seeds and monosaccharide ligands were analysed by isothermal titration calorimetry and surface plasmon resonance. The results are consistent with the lectin bearing three thermodynamically identical binding sites for mannose/glucose per monomer with dissociation constants in the millimolar range. Binding of each ligand by the lectin is enthalpically driven. Crystals have been obtained of the lectin in complex with a brominated derivative of mannose (5-bromo-4-chloro-3-indolyl-alpha-D-mannose), which were suitable for deriving an electron-density map by MAD phasing. In agreement with the thermodynamic data, six Br atoms were found in the asymmetric unit of the monoclinic P2(1) crystals, which contained two P. Platycephala lectin molecules. The availability of other Br derivatives of monosaccharides (glucose, galactose, fucose) may make this strategy widely useful for structure elucidation of novel lectins or when (as in the case of the P. Platycephala lectin) molecular-replacement methods fail.
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Crystallization and preliminary X-ray diffraction analysis of the seed lectin from Parkia Platycephala.
Acta Crystallographica Section D Biological Crystallography, 2001Co-Authors: Francisca Gallego Del Sol, Thalles B. Grangeiro, Benildo Sousa Cavada, Celso Shiniti Nagano, Santiago Ramón-maiques, Cláudia F. Santos, Creuza M. S. A. Farias, Juan J. CalveteAbstract:The crystallization and preliminary X-ray diffraction analysis of the seed lectin of Parkia Platycephala, a Mimosoideae, regarded as the most primitive group of the Leguminosae plants, are reported. Its amino-acid sequence consists of three tandemly arranged jacalin-related β-prism domains, which is a novel fold for a leguminous lectin. Furthermore, no other lectin structure with this arrangement of domains has been described. P212121 crystals (unit-cell parameters a = 63.6, b = 68.5, c = 208.5 A), which diffract to a maximum resolution of 2.2 A, were obtained in hanging drops at pH 8 and 293 K by the vapor-diffusion method using 10% 2-propanol and 20% polyethylene glycol 4000 as precipitants. The asymmetric unit contains two lectin molecules and has a solvent content of 46%. Only a single β-prism domain could be located by molecular replacement using the structure of the Helianthus tuberosus lectin (PDB code 1c3k) as the search model. Isomorphous heavy-atom derivatives are currently being produced to solve the complete structure of the P. Platycephala seed lectin.
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Crystallization and preliminary X-ray diffraction analysis of the seed lectin from Parkia Platycephala.
Acta crystallographica. Section D Biological crystallography, 2001Co-Authors: Francisca Gallego Del Sol, Thalles B. Grangeiro, Celso S Nagano, Benildo S Cavada, Santiago Ramón-maiques, Cláudia F. Santos, Creuza M. S. A. Farias, Juan J. CalveteAbstract:The crystallization and preliminary X-ray diffraction analysis of the seed lectin of Parkia Platycephala, a Mimosoideae, regarded as the most primitive group of the Leguminosae plants, are reported. Its amino-acid sequence consists of three tandemly arranged jacalin-related beta-prism domains, which is a novel fold for a leguminous lectin. Furthermore, no other lectin structure with this arrangement of domains has been described. P2(1)2(1)2(1) crystals (unit-cell parameters a = 63.6, b = 68.5, c = 208.5 A), which diffract to a maximum resolution of 2.2 A, were obtained in hanging drops at pH 8 and 293 K by the vapor-diffusion method using 10% 2-propanol and 20% polyethylene glycol 4000 as precipitants. The asymmetric unit contains two lectin molecules and has a solvent content of 46%. Only a single beta-prism domain could be located by molecular replacement using the structure of the Helianthus tuberosus lectin (PDB code 1c3k) as the search model. Isomorphous heavy-atom derivatives are currently being produced to solve the complete structure of the P. Platycephala seed lectin.
Francisca Gallego Del Sol - One of the best experts on this subject based on the ideXlab platform.
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The First Crystal Structure of a Mimosoideae Lectin Reveals a Novel Quaternary Arrangement of a Widespread Domain
Journal of Molecular Biology, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Juan J. CalveteAbstract:The crystal structures of the apo and mannose-bound Parkia Platycephala seed lectin represent the first structure of a Mimosoideae lectin and a novel circular arrangement of β-prism domains, and highlight the adaptability of the β-prism fold as a building block in the evolution of plant lectins. The P. Platycephala lectin is a dimer both in solution and in the crystals. Mannose binding to each of the three homologous carbohydrate-recognition domains of the lectin occurs through different modes, and restrains the flexibility of surface-exposed loops and residues involved in carbohydrate recognition. The planar array of carbohydrate-binding sites on the rim of the toroid-shaped structure of the P. Platycephala lectin dimer immediately suggests a mechanism to promote multivalent interactions leading to cross-linking of carbohydrate ligands as part of the host strategy against phytopredators and pathogens. The cyclic structure of the P. Platycephala lectin points to the convergent evolution of a structural principle for the construction of lectins involved in host defense or in attacking other organisms.
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Energetics of 5-bromo-4-chloro-3-indolyl-α-d-mannose binding to the Parkia Platycephala seed lectin and its use for MAD phasing
Acta Crystallographica Section F Structural Biology and Crystallization Communications, 2005Co-Authors: Francisca Gallego Del Sol, Benildo Sousa Cavada, Celso Shiniti Nagano, Javier Gómez, Sylviane Hoos, Patrick England, Juan J. CalveteAbstract:Parkia Platycephala belongs to the most primitive group of Leguminosae plants. Its seed lectin is made up of three homologous β-prism repeats and exhibits binding specificity for mannose/glucose. The properties of the association between the lectin from P. Platycephala seeds and monosaccharide ligands were analysed by isothermal titration calorimetry and surface plasmon resonance. The results are consistent with the lectin bearing three thermodynamically identical binding sites for mannose/glucose per monomer with dissociation constants in the millimolar range. Binding of each ligand by the lectin is enthalpically driven. Crystals have been obtained of the lectin in complex with a brominated derivative of mannose (5-bromo-4-chloro-3-indolyl-α-d-mannose), which were suitable for deriving an electron-density map by MAD phasing. In agreement with the thermodynamic data, six Br atoms were found in the asymmetric unit of the monoclinic P21 crystals, which contained two P. Platycephala lectin molecules. The availability of other Br derivatives of monosaccharides (glucose, galactose, fucose) may make this strategy widely useful for structure elucidation of novel lectins or when (as in the case of the P. Platycephala lectin) molecular-replacement methods fail.
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Crystallization and preliminary X-ray diffraction analysis of the seed lectin from Parkia Platycephala.
Acta Crystallographica Section D Biological Crystallography, 2001Co-Authors: Francisca Gallego Del Sol, Thalles B. Grangeiro, Benildo Sousa Cavada, Celso Shiniti Nagano, Santiago Ramón-maiques, Cláudia F. Santos, Creuza M. S. A. Farias, Juan J. CalveteAbstract:The crystallization and preliminary X-ray diffraction analysis of the seed lectin of Parkia Platycephala, a Mimosoideae, regarded as the most primitive group of the Leguminosae plants, are reported. Its amino-acid sequence consists of three tandemly arranged jacalin-related β-prism domains, which is a novel fold for a leguminous lectin. Furthermore, no other lectin structure with this arrangement of domains has been described. P212121 crystals (unit-cell parameters a = 63.6, b = 68.5, c = 208.5 A), which diffract to a maximum resolution of 2.2 A, were obtained in hanging drops at pH 8 and 293 K by the vapor-diffusion method using 10% 2-propanol and 20% polyethylene glycol 4000 as precipitants. The asymmetric unit contains two lectin molecules and has a solvent content of 46%. Only a single β-prism domain could be located by molecular replacement using the structure of the Helianthus tuberosus lectin (PDB code 1c3k) as the search model. Isomorphous heavy-atom derivatives are currently being produced to solve the complete structure of the P. Platycephala seed lectin.
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The amino-acid sequence of the glucose/mannose-specific lectin isolated from Parkia Platycephala seeds reveals three tandemly arranged jacalin-related domains
European journal of biochemistry, 2001Co-Authors: Karlheinz Mann, Thalles B. Grangeiro, Benildo Sousa Cavada, Celso Shiniti Nagano, Francisca Gallego Del Sol, Cláudia F. Santos, Creuza M. S. A. Farias, Juan J. CalveteAbstract:A mannose/glucose-specific lectin was isolated from seeds of Parkia Platycephala, the most primitive subfamily of Leguminosae plants. The molecular mass of the purified lectin determined by mass spectrometry was 47 946 +/- 6 Da (by electrospray ionization) and 47 951 +/- 9 Da (by matrix-assisted laser-desoption ionization). The apparent molecular mass of the lectin in solutions of pH in the range 4.5-8.5 determined by analytical ultracentrifugation equilibrium sedimentation was 94 +/- 3 kDa, showing that the protein behaved as a non-pH-dependent dimer. The amino-acid sequence of the Parkia lectin was determined by Edman degradation of overlapping peptides. This is the first report of the primary structure of a Mimosoideae lectin. The protein contained a blocked N-terminus and a single, nonglycosylated polypeptide chain composed of three tandemly arranged homologous domains. Each of these domains shares sequence similarity with jacalin-related lectin monomers from Asteraceae, Convolvulaceae, Moraceae, Musaceae, Gramineae, and Fagaceae plant families. Based on this homology, we predict that each Parkia lectin repeat may display a beta prism fold similar to that observed in the crystal structure of the lectin from Helianthus tuberosus. The P. Platycephala lectin also shows sequence similarity with stress- and pathogen-upregulated defence genes of a number of different plants, suggesting a common ancestry for jacalin-related lectins and inducible defence proteins.
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the amino acid sequence of the glucose mannose specific lectin isolated from parkia Platycephala seeds reveals three tandemly arranged jacalin related domains
FEBS Journal, 2001Co-Authors: Karlheinz Mann, Thalles B. Grangeiro, Benildo Sousa Cavada, Celso Shiniti Nagano, Francisca Gallego Del Sol, Cláudia F. Santos, Creuza M. S. A. Farias, Juan J. CalveteAbstract:A mannose/glucose-specific lectin was isolated from seeds of Parkia Platycephala, the most primitive subfamily of Leguminosae plants. The molecular mass of the purified lectin determined by mass spectrometry was 47 946 +/- 6 Da (by electrospray ionization) and 47 951 +/- 9 Da (by matrix-assisted laser-desoption ionization). The apparent molecular mass of the lectin in solutions of pH in the range 4.5-8.5 determined by analytical ultracentrifugation equilibrium sedimentation was 94 +/- 3 kDa, showing that the protein behaved as a non-pH-dependent dimer. The amino-acid sequence of the Parkia lectin was determined by Edman degradation of overlapping peptides. This is the first report of the primary structure of a Mimosoideae lectin. The protein contained a blocked N-terminus and a single, nonglycosylated polypeptide chain composed of three tandemly arranged homologous domains. Each of these domains shares sequence similarity with jacalin-related lectin monomers from Asteraceae, Convolvulaceae, Moraceae, Musaceae, Gramineae, and Fagaceae plant families. Based on this homology, we predict that each Parkia lectin repeat may display a beta prism fold similar to that observed in the crystal structure of the lectin from Helianthus tuberosus. The P. Platycephala lectin also shows sequence similarity with stress- and pathogen-upregulated defence genes of a number of different plants, suggesting a common ancestry for jacalin-related lectins and inducible defence proteins.
Cosmo Rufino De ,lima - One of the best experts on this subject based on the ideXlab platform.
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UMEDECIMENTO DO SUBSTRATO E TEMPERATURA NA GERMINAÇÃO DE SEMENTES DE Parkia Platycephala BENTH.
'Universidad Federal de Santa Maria', 2015Co-Authors: Gonçalves, Edilma Pereira, Pablo Radamés Cabral De ,frança, Viana, Jeandson Silva, Alves, Edna Ursulino, Guedes, Roberta Sales, Cosmo Rufino De ,limaAbstract:The Parkia Platycephala Benth. (faveira) is a leguminous tree, known as a provider of commercial wood in the Amazon rain forest. This study aimed to evaluate the effects of different volumes of water for substrate moisture and temperatures on germination of Parkia Platycephala. After this, they were sowing over towel paper, organized in rolls wetted with water contents equivalent to 2.0; 2.5; 3.0 and 3.5 times the weight of the substrate without new water addition, and they were maintained in chambers at constant temperatures of 20, 25, 30°C and alternate temperature 20-30°C. The following parameters were analyzed: the germination percentage, first count germination, index of germination speed, length and dry mass of seedlings (shoot and root). A completely randomized design was used with a 4 x 4 factorial (water volumes and temperatures). The moistening of the substrate with 2.0, 2.5, 3.0 and 3.5 times the weight of the paper at temperatures of 25, 30 and 20-30 ºC can be used for germination and vigor of Parkia Platycephala Benth. The temperature of 20ºC and all volumes of water tested for wetting the substrate reduced the germination and the vigor of these seeds.http://dx.doi.org/10.5902/1980509819607A Parkia Platycephala Benth. (faveira) é uma leguminosa arbórea, conhecida como fornecedora de madeiracomercial na Amazônia. O presente trabalho foi conduzido com o objetivo de avaliar diferentes volumesde água para umedecimento do substrato e temperaturas na germinação e vigor de sementes de Parkia Platycephala. As sementes foram submetidas ao teste de germinação em papel-toalha, organizado naforma de rolos e umedecido com volumes de água equivalentes a 2,0; 2,5; 3,0 e 3,5 vezes o peso seco dosubstrato e colocadas nas temperaturas constantes de 20, 25, 30 e alternada de 20-30°C. Foram avaliados: aporcentagem de germinação, a primeira contagem de germinação e o índice de velocidade de germinação,o comprimento e a massa seca da raiz e da parte aérea das plântulas normais. O delineamento experimentalfoi o inteiramente ao acaso, com os tratamentos distribuídos em esquema fatorial 4 x 4 (quatro volumesde água e quatro temperaturas). O umedecimento do substrato com 2,0; 2,5; 3,0 e 3,5 vezes o peso dopapel nas temperaturas de 25, 30 e 20-30ºC pode ser utilizado para avaliação da germinação e vigor dassementes de Parkia Platycephala Benth. A temperatura de 20ºC em todos os volumes de água testados paraumedecimento do substrato reduziu a germinação e o vigor das sementes
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umedecimento do substrato e temperatura na germinacao de sementes de parkia Platycephala benth
Ciencia Florestal, 2015Co-Authors: Edilma Pereira Goncalves, Pablo Radamés Cabral De ,frança, Jeandson Silva Viana, Edna Ursulino Alves, Roberta Sales Guedes, Cosmo Rufino De ,limaAbstract:The Parkia Platycephala Benth. (faveira) is a leguminous tree, known as a provider of commercial wood in the Amazon rain forest. This study aimed to evaluate the effects of different volumes of water for substrate moisture and temperatures on germination of Parkia Platycephala . After this, they were sowing over towel paper, organized in rolls wetted with water contents equivalent to 2.0; 2.5; 3.0 and 3.5 times the weight of the substrate without new water addition, and they were maintained in chambers at constant temperatures of 20, 25, 30°C and alternate temperature 20-30°C. The following parameters were analyzed: the germination percentage, first count germination, index of germination speed, length and dry mass of seedlings (shoot and root). A completely randomized design was used with a 4 x 4 factorial (water volumes and temperatures). The moistening of the substrate with 2.0, 2.5, 3.0 and 3.5 times the weight of the paper at temperatures of 25, 30 and 20-30 oC can be used for germination and vigor of Parkia Platycephala Benth. The temperature of 20oC and all volumes of water tested for wetting the substrate reduced the germination and the vigor of these seeds.
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UMEDECIMENTO DO SUBSTRATO E TEMPERATURA NA GERMINAÇÃO DE SEMENTES DE Parkia Platycephala BENTH.
Universidade Federal de Santa Maria, 2015Co-Authors: Gonçalves, Edilma Pereira, Pablo Radamés Cabral De ,frança, Viana, Jeandson Silva, Alves, Edna Ursulino, Guedes, Roberta Sales, Cosmo Rufino De ,limaAbstract:RESUMO A Parkia Platycephala Benth. (faveira) é uma leguminosa arbórea, conhecida como fornecedora de madeira comercial na Amazônia. O presente trabalho foi conduzido com o objetivo de avaliar diferentes volumes de água para umedecimento do substrato e temperaturas na germinação e vigor de sementes deParkia Platycephala. As sementes foram submetidas ao teste de germinação em papel-toalha, organizado na forma de rolos e umedecido com volumes de água equivalentes a 2,0; 2,5; 3,0 e 3,5 vezes o peso seco do substrato e colocadas nas temperaturas constantes de 20, 25, 30 e alternada de 20-30°C. Foram avaliados: a porcentagem de germinação, a primeira contagem de germinação e o índice de velocidade de germinação, o comprimento e a massa seca da raiz e da parte aérea das plântulas normais. O delineamento experimental foi o inteiramente ao acaso, com os tratamentos distribuídos em esquema fatorial 4 x 4 (quatro volumes de água e quatro temperaturas). O umedecimento do substrato com 2,0; 2,5; 3,0 e 3,5 vezes o peso do papel nas temperaturas de 25, 30 e 20-30ºC pode ser utilizado para avaliação da germinação e vigor das sementes deParkia Platycephala Benth. A temperatura de 20ºC em todos os volumes de água testados para umedecimento do substrato reduziu a germinação e o vigor das sementes