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Product Summary
Fragment
Full length
Protein Description
Phosphoglycerate Mutase 1
Background
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.
Protein Classification
isomerase hydrase
Structure Weight
361525.84 Da
PDBID
1YJX
Method
X-Ray Diffraction
Resolution
2.8 Å
Ligand Chemical Component
citric acid; chloride ion
Reference
Wang, Y., Wei, Z., Liu, L., Cheng, Z., Lin, Y., Ji, F., Gong, W. (2005) Crystal structure of human B-type phosphoglycerate mutase bound with citrate. Biochem.Biophys.Res.Commun. 331: 1207-1215
cDNALength
786