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Joseph Parello - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of the unique Parvalbumin component from muscle of the leopard shark triakis semifasciata the first x ray study of an alpha Parvalbumin
Journal of Molecular Biology, 1993Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
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Crystal structure of the unique Parvalbumin component from muscle of the leopard shark (Triakis semifasciata)
Journal of Molecular Biology, 1992Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
Françoise Roquet - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of the unique Parvalbumin component from muscle of the leopard shark triakis semifasciata the first x ray study of an alpha Parvalbumin
Journal of Molecular Biology, 1993Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
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Crystal structure of the unique Parvalbumin component from muscle of the leopard shark (Triakis semifasciata)
Journal of Molecular Biology, 1992Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
Jean-claude Rambaud - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of the unique Parvalbumin component from muscle of the leopard shark triakis semifasciata the first x ray study of an alpha Parvalbumin
Journal of Molecular Biology, 1993Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
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Crystal structure of the unique Parvalbumin component from muscle of the leopard shark (Triakis semifasciata)
Journal of Molecular Biology, 1992Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
Bernard Tinant - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of the unique Parvalbumin component from muscle of the leopard shark triakis semifasciata the first x ray study of an alpha Parvalbumin
Journal of Molecular Biology, 1993Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
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Crystal structure of the unique Parvalbumin component from muscle of the leopard shark (Triakis semifasciata)
Journal of Molecular Biology, 1992Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
Jean-paul Declercq - One of the best experts on this subject based on the ideXlab platform.
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crystal structure of the unique Parvalbumin component from muscle of the leopard shark triakis semifasciata the first x ray study of an alpha Parvalbumin
Journal of Molecular Biology, 1993Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
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Crystal structure of the unique Parvalbumin component from muscle of the leopard shark (Triakis semifasciata)
Journal of Molecular Biology, 1992Co-Authors: Françoise Roquet, Jean-paul Declercq, Bernard Tinant, Jean-claude Rambaud, Joseph ParelloAbstract:The three-dimensional structure of Parvalbumin from leopard shark (Triakis semifasciata) with 109 amino acid residues (alpha-series) is described at 1.54 A resolution. Crystals were grown at 20 degrees C from 2.9 M-potassium/sodium phosphate solutions at pH 5.6. The space group is P3(1)21 and unit cell dimensions are a = b = 32.12 A and c = 149.0 A. The structure has been solved by the molecular replacement method using pike 4.10 Parvalbumin as a model. The final structure refinement resulted in an R-factor of 17.3% for 11,363 independent reflections at 1.54 A resolution. The shark Parvalbumin shows the main features of all Parvalbumins: the folding of the chain including six alpha-helices, the salt bridge between Arg75 and Glu81, and the hydrophobic core. Compared to the structure of beta-Parvalbumins from pike and carp, one main difference is observed: the chain is one residue longer and this additional residue, which extends the F helix, is involved through its C-terminal carboxylate group in a network of electrostatic contacts with two basic residues, His31 in the B helix and Lys36 in the BC segment. Furthermore, hydrogen bonds exist between the side-chains of Gln108 (F helix) and Tyr26 (B helix). There is therefore a "locking" of the tertiary structure through contacts between two sequentially distant regions in the protein and this is likely to contribute to making the stability of an alpha-Parvalbumin higher in comparison to that of a beta-Parvalbumin. The lengthening of the C-terminal F helix by one residue appears to be a major feature of alpha-Parvalbumins in general, owing to the homologies of the amino acid sequences. Besides the lengthening of the C-terminal helix, the classification of the leopard shark Parvalbumin in the alpha-series rests upon the observation of Lys13, Leu32, Glu61 and Val66. As this is the first crystal structure description of a Parvalbumin from the alpha-phylogenetic lineage, it was hoped that it would clearly determine the presence or absence of a third cation binding site in Parvalbumins belonging to the alpha-lineage. In beta-pike pI 4.10 Parvalbumin, Asp61 participates as a direct ligand of a third site, the satellite of the CD site. In shark Parvalbumin, as in nearly all alpha-Parvalbumins, one finds Glu at position 61. Unfortunately, the conformation of the polar head of Glu61 cannot be inferred from the X-ray data.(ABSTRACT TRUNCATED AT 400 WORDS)
