Cat. No.

CBCRY11

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.

Molecular description

Protein Classification

isomerase hydrase

Structure Weight

361525.84

Polymer

1

Molecule

Phosphoglycerate mutase 1

Chain Length

262 amino acids

Crystal Description

PDB ID

1YJX 

MMDB ID

33356

Source

E.coli

Method

X-Ray Diffraction

Resolution

2.8 Å

Ligand Chemical Component

citric acid; chloride ion

Gene information

Gene Name

PGAM1

Synonyms

PGAMA; PGAM-B; PGAM1; RP11-452K12.8; OTTHUMP00000020190; OTTHUMP00000059414; phosphoglycerate mutase A, nonmuscle form; EC 5.4.2.1,EC 5.4.2.4,EC 3.1.3.13; BPG-dependent PGAM 1; Phosphoglycerate mutase isozyme B; phosphoglycerate mutase A, nonmuscle form

UniProt ID

P18669

GeneID

5223

Chromosome  Location

10q25.3

Function

bisphosphoglycerate 2-phosphatase activity; bisphosphoglycerate mutase activity; hydrolase activity; isomerase activity; phosphoglycerate mutase activity; protein kinase binding

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