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Andrzej Joachimiak - One of the best experts on this subject based on the ideXlab platform.
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Streptococcus Pneumonia YlxR at 1.35 A shows a putative new fold.
Acta Crystallographica Section D Biological Crystallography, 2001Co-Authors: Jerzy Osipiuk, Piotr Gornicki, Luke Maj, Irina Dementieva, Roman A. Laskowski, Andrzej JoachimiakAbstract:The structure of the YlxR protein of unknown function from Streptococcus Pneumonia was determined to 1.35 A. YlxR is expressed from the nusA/infB operon in bacteria and belongs to a small protein family (COG2740) that shares a conserved sequence motif GRGA(Y/W). The family shows no significant amino-acid sequence similarity with other proteins. Three-wavelength diffraction MAD data were collected to 1.7 A from orthorhombic crystals using synchrotron radiation and the structure was determined using a semi-automated approach. The YlxR structure resembles a two-layer α/β sandwich with the overall shape of a cylinder and shows no structural homology to proteins of known structure. Structural analysis revealed that the YlxR structure represents a new protein fold that belongs to the α–β plait superfamily. The distribution of the electrostatic surface potential shows a large positively charged patch on one side of the protein, a feature often found in nucleic acid-binding proteins. Three sulfate ions bind to this positively charged surface. Analysis of potential binding sites uncovered several substantial clefts, with the largest spanning 3/4 of the protein. A similar distribution of binding sites and a large sharply bent cleft are observed in RNA-binding proteins that are unrelated in sequence and structure. It is proposed that YlxR is an RNA-binding protein.
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Streptococcus Pneumonia YlxR at 1.35 A shows a putative new fold.
Acta crystallographica. Section D Biological crystallography, 2001Co-Authors: Jerzy Osipiuk, Piotr Gornicki, Luke Maj, Irina Dementieva, R Laskowski, Andrzej JoachimiakAbstract:The structure of the YlxR protein of unknown function from Streptococcus Pneumonia was determined to 1.35 A. YlxR is expressed from the nusA/infB operon in bacteria and belongs to a small protein family (COG2740) that shares a conserved sequence motif GRGA(Y/W). The family shows no significant amino-acid sequence similarity with other proteins. Three-wavelength diffraction MAD data were collected to 1.7 A from orthorhombic crystals using synchrotron radiation and the structure was determined using a semi-automated approach. The YlxR structure resembles a two-layer alpha/beta sandwich with the overall shape of a cylinder and shows no structural homology to proteins of known structure. Structural analysis revealed that the YlxR structure represents a new protein fold that belongs to the alpha-beta plait superfamily. The distribution of the electrostatic surface potential shows a large positively charged patch on one side of the protein, a feature often found in nucleic acid-binding proteins. Three sulfate ions bind to this positively charged surface. Analysis of potential binding sites uncovered several substantial clefts, with the largest spanning 3/4 of the protein. A similar distribution of binding sites and a large sharply bent cleft are observed in RNA-binding proteins that are unrelated in sequence and structure. It is proposed that YlxR is an RNA-binding protein.
Zonggang Chen - One of the best experts on this subject based on the ideXlab platform.
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Exploring the broad nucleotide triphosphate and sugar-1-phosphate specificity of thymidylyltransferase Cps23FL from Streptococcus Pneumonia serotype 23F
RSC Advances, 2020Co-Authors: Hong Wang, Guoxia Jin, Zonggang ChenAbstract:Glucose-1-phosphate thymidylyltransferase (Cps23FL) from Streptococcus Pneumonia serotype 23F is the initial enzyme that catalyses the thymidylyl transfer reaction in prokaryotic deoxythymidine diphosphate-L-rhamnose (dTDP-Rha) biosynthetic pathway. In this study, the broad substrate specificity of Cps23FL towards six glucose-1-phosphates and nine nucleoside triphosphates as substrates was systematically explored, eventually providing access to nineteen sugar nucleotide analogs.
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Biochemical studies of a β-1,4-rhamnoslytransferase from Streptococcus Pneumonia serotype 23F
Organic & biomolecular chemistry, 2019Co-Authors: Hong Wang, Chenghe Xiong, Guoxia Jin, Zonggang Chen, Zhongwu GuoAbstract:A new β-rhamnoslytransferase Cps23FT from Streptococcus Pneumonia serotype 23F was expressed and characterized. Its enzymatic activity and function were confirmed for the first time by utilizing enzymatically prepared dTDP-Rha and chemically synthesized Glcα-PP-(CH2)11-OPh as substrates. This reaction gave the desired disaccharide Rhaβ-1,4-Glcα-PP-(CH2)11-OPh in a good isolated yield (67%), suggesting the potential of Cps23FT as a tool enzyme for the synthesis of complex oligosaccharides containing difficult β-rhamnosyl linkages. Furthermore, site-directed mutagenesis of Cps23FT disclosed that its 271DKD273 motif was critical for the enzymatic activity and most likely the binding site for the required divalent metal cation.
Hong Wang - One of the best experts on this subject based on the ideXlab platform.
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Exploring the broad nucleotide triphosphate and sugar-1-phosphate specificity of thymidylyltransferase Cps23FL from Streptococcus Pneumonia serotype 23F
RSC Advances, 2020Co-Authors: Hong Wang, Guoxia Jin, Zonggang ChenAbstract:Glucose-1-phosphate thymidylyltransferase (Cps23FL) from Streptococcus Pneumonia serotype 23F is the initial enzyme that catalyses the thymidylyl transfer reaction in prokaryotic deoxythymidine diphosphate-L-rhamnose (dTDP-Rha) biosynthetic pathway. In this study, the broad substrate specificity of Cps23FL towards six glucose-1-phosphates and nine nucleoside triphosphates as substrates was systematically explored, eventually providing access to nineteen sugar nucleotide analogs.
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Biochemical studies of a β-1,4-rhamnoslytransferase from Streptococcus Pneumonia serotype 23F
Organic & biomolecular chemistry, 2019Co-Authors: Hong Wang, Chenghe Xiong, Guoxia Jin, Zonggang Chen, Zhongwu GuoAbstract:A new β-rhamnoslytransferase Cps23FT from Streptococcus Pneumonia serotype 23F was expressed and characterized. Its enzymatic activity and function were confirmed for the first time by utilizing enzymatically prepared dTDP-Rha and chemically synthesized Glcα-PP-(CH2)11-OPh as substrates. This reaction gave the desired disaccharide Rhaβ-1,4-Glcα-PP-(CH2)11-OPh in a good isolated yield (67%), suggesting the potential of Cps23FT as a tool enzyme for the synthesis of complex oligosaccharides containing difficult β-rhamnosyl linkages. Furthermore, site-directed mutagenesis of Cps23FT disclosed that its 271DKD273 motif was critical for the enzymatic activity and most likely the binding site for the required divalent metal cation.
Jerzy Osipiuk - One of the best experts on this subject based on the ideXlab platform.
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Streptococcus Pneumonia YlxR at 1.35 A shows a putative new fold.
Acta Crystallographica Section D Biological Crystallography, 2001Co-Authors: Jerzy Osipiuk, Piotr Gornicki, Luke Maj, Irina Dementieva, Roman A. Laskowski, Andrzej JoachimiakAbstract:The structure of the YlxR protein of unknown function from Streptococcus Pneumonia was determined to 1.35 A. YlxR is expressed from the nusA/infB operon in bacteria and belongs to a small protein family (COG2740) that shares a conserved sequence motif GRGA(Y/W). The family shows no significant amino-acid sequence similarity with other proteins. Three-wavelength diffraction MAD data were collected to 1.7 A from orthorhombic crystals using synchrotron radiation and the structure was determined using a semi-automated approach. The YlxR structure resembles a two-layer α/β sandwich with the overall shape of a cylinder and shows no structural homology to proteins of known structure. Structural analysis revealed that the YlxR structure represents a new protein fold that belongs to the α–β plait superfamily. The distribution of the electrostatic surface potential shows a large positively charged patch on one side of the protein, a feature often found in nucleic acid-binding proteins. Three sulfate ions bind to this positively charged surface. Analysis of potential binding sites uncovered several substantial clefts, with the largest spanning 3/4 of the protein. A similar distribution of binding sites and a large sharply bent cleft are observed in RNA-binding proteins that are unrelated in sequence and structure. It is proposed that YlxR is an RNA-binding protein.
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Streptococcus Pneumonia YlxR at 1.35 A shows a putative new fold.
Acta crystallographica. Section D Biological crystallography, 2001Co-Authors: Jerzy Osipiuk, Piotr Gornicki, Luke Maj, Irina Dementieva, R Laskowski, Andrzej JoachimiakAbstract:The structure of the YlxR protein of unknown function from Streptococcus Pneumonia was determined to 1.35 A. YlxR is expressed from the nusA/infB operon in bacteria and belongs to a small protein family (COG2740) that shares a conserved sequence motif GRGA(Y/W). The family shows no significant amino-acid sequence similarity with other proteins. Three-wavelength diffraction MAD data were collected to 1.7 A from orthorhombic crystals using synchrotron radiation and the structure was determined using a semi-automated approach. The YlxR structure resembles a two-layer alpha/beta sandwich with the overall shape of a cylinder and shows no structural homology to proteins of known structure. Structural analysis revealed that the YlxR structure represents a new protein fold that belongs to the alpha-beta plait superfamily. The distribution of the electrostatic surface potential shows a large positively charged patch on one side of the protein, a feature often found in nucleic acid-binding proteins. Three sulfate ions bind to this positively charged surface. Analysis of potential binding sites uncovered several substantial clefts, with the largest spanning 3/4 of the protein. A similar distribution of binding sites and a large sharply bent cleft are observed in RNA-binding proteins that are unrelated in sequence and structure. It is proposed that YlxR is an RNA-binding protein.
Guoxia Jin - One of the best experts on this subject based on the ideXlab platform.
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Exploring the broad nucleotide triphosphate and sugar-1-phosphate specificity of thymidylyltransferase Cps23FL from Streptococcus Pneumonia serotype 23F
RSC Advances, 2020Co-Authors: Hong Wang, Guoxia Jin, Zonggang ChenAbstract:Glucose-1-phosphate thymidylyltransferase (Cps23FL) from Streptococcus Pneumonia serotype 23F is the initial enzyme that catalyses the thymidylyl transfer reaction in prokaryotic deoxythymidine diphosphate-L-rhamnose (dTDP-Rha) biosynthetic pathway. In this study, the broad substrate specificity of Cps23FL towards six glucose-1-phosphates and nine nucleoside triphosphates as substrates was systematically explored, eventually providing access to nineteen sugar nucleotide analogs.
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Biochemical studies of a β-1,4-rhamnoslytransferase from Streptococcus Pneumonia serotype 23F
Organic & biomolecular chemistry, 2019Co-Authors: Hong Wang, Chenghe Xiong, Guoxia Jin, Zonggang Chen, Zhongwu GuoAbstract:A new β-rhamnoslytransferase Cps23FT from Streptococcus Pneumonia serotype 23F was expressed and characterized. Its enzymatic activity and function were confirmed for the first time by utilizing enzymatically prepared dTDP-Rha and chemically synthesized Glcα-PP-(CH2)11-OPh as substrates. This reaction gave the desired disaccharide Rhaβ-1,4-Glcα-PP-(CH2)11-OPh in a good isolated yield (67%), suggesting the potential of Cps23FT as a tool enzyme for the synthesis of complex oligosaccharides containing difficult β-rhamnosyl linkages. Furthermore, site-directed mutagenesis of Cps23FT disclosed that its 271DKD273 motif was critical for the enzymatic activity and most likely the binding site for the required divalent metal cation.