1yjx

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'''Crystal structure of human B type phosphoglycerate mutase'''<br />
'''Crystal structure of human B type phosphoglycerate mutase'''<br />
==Overview==
==Overview==
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The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes, the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in, glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as, the cofactor. The crystal structures of human dPGM-B bound with citrate, were determined in two crystal forms. These structures reveal a, dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate, mutase), based on which a dPGM/BPGM heterodimer structure is proposed., Structural comparison supports that the conformational changes of residues, 13-21 and 98-117 determine PGM/BPGM activity differences. The, citrate-binding mode suggests a substrate-binding model, consistent with, the structure of Escherichia coli dPGM/vanadate complex. A chloride ion, was found in the center of the dimer, providing explanation for the, contribution of chloride ion to dPGM activities. Based on the structural, information, the possible reasons for the deficient human dPGM mutations, found in some patients are also discussed.
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The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor. The crystal structures of human dPGM-B bound with citrate were determined in two crystal forms. These structures reveal a dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate mutase), based on which a dPGM/BPGM heterodimer structure is proposed. Structural comparison supports that the conformational changes of residues 13-21 and 98-117 determine PGM/BPGM activity differences. The citrate-binding mode suggests a substrate-binding model, consistent with the structure of Escherichia coli dPGM/vanadate complex. A chloride ion was found in the center of the dimer, providing explanation for the contribution of chloride ion to dPGM activities. Based on the structural information, the possible reasons for the deficient human dPGM mutations found in some patients are also discussed.
==About this Structure==
==About this Structure==
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1YJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YJX OCA].
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1YJX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YJX OCA].
==Reference==
==Reference==
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[[Category: alpha/beta]]
[[Category: alpha/beta]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:21:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:06:04 2008''

Revision as of 14:06, 21 February 2008

Image:1yjx.gif

1yjx, resolution 2.800Å

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Crystal structure of human B type phosphoglycerate mutase

Overview

The B-type cofactor-dependent phosphoglycerate mutase (dPGM-B) catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in glycolysis and gluconeogenesis pathways using 2,3-bisphosphoglycerate as the cofactor. The crystal structures of human dPGM-B bound with citrate were determined in two crystal forms. These structures reveal a dimerization mode conserved in both of dPGM and BPGM (bisphosphoglycerate mutase), based on which a dPGM/BPGM heterodimer structure is proposed. Structural comparison supports that the conformational changes of residues 13-21 and 98-117 determine PGM/BPGM activity differences. The citrate-binding mode suggests a substrate-binding model, consistent with the structure of Escherichia coli dPGM/vanadate complex. A chloride ion was found in the center of the dimer, providing explanation for the contribution of chloride ion to dPGM activities. Based on the structural information, the possible reasons for the deficient human dPGM mutations found in some patients are also discussed.

About this Structure

1YJX is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human B-type phosphoglycerate mutase bound with citrate., Wang Y, Wei Z, Liu L, Cheng Z, Lin Y, Ji F, Gong W, Biochem Biophys Res Commun. 2005 Jun 17;331(4):1207-15. PMID:15883004

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