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2,3-diphosphoglycerate |
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H(2)O |
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![]() 3-phosphoglycerate |
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![]() phosphate |
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![]() 2-phospho-D-glycerate |
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2,3-diphosphoglycerate |
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![]() 3-phospho-D-glycerate |
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![]() 2,3-diphosphoglycerate 2-phospho-D-glycerate |
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![]() 3-phospho-D-glycerate |
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![]() 3-phospho-D-glyceroyl phosphate |
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![]() 2,3-bisphospho-D-glycerate |
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Key reference
DOI no: 10.1016/j.bbrc.2005.03.243 Biochem Biophys Res Commun 331:1207-1215 (2005) PubMed id: 15883004 ![]()
Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Y.Wang, Z.Wei, L.Liu, Z.Cheng, Y.Lin, F.Ji, W.Gong. ![]()
ABSTRACT ![]()
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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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Literature references that cite this PDB file's key reference
PubMed id Reference
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17579775 M.J.Evans, G.M.Morris, J.Wu, A.J.Olson, E.J.Sorensen, and B.F.Cravatt (2007).
Mechanistic and structural requirements for active site labeling of phosphoglycerate mutase by spiroepoxides.Mol Biosyst, 3, 495-506.
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16672613 H.A.Watkins, and E.N.Baker (2006).
Structural and functional analysis of Rv3214 from Mycobacterium tuberculosis, a protein with conflicting functional annotations, leads to its characterization as a phosphatase.J Bacteriol, 188, 3589-3599.
PDB code: 2a6p 16880558 N.K.Lokanath, and N.Kunishima (2006).
Purification, crystallization and preliminary X-ray crystallographic analysis of the archaeal phosphoglycerate mutase PH0037 from Pyrococcus horikoshii OT3.Acta Crystallogr Sect F Struct Biol Cryst Commun, 62, 788-790.
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17052986 Y.Wang, L.Liu, Z.Wei, Z.Cheng, Y.Lin, and W.Gong (2006).
Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase.J Biol Chem, 281, 39642-39648.
PDB codes: 2a9j 2f90 2h4x 2h4z 2h52 2hhj
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16200062 M.J.Evans, A.Saghatelian, E.J.Sorensen, and B.F.Cravatt (2005).
Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling.Nat Biotechnol, 23, 1303-1307. The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.