Creative Biostructure

Online Inquiry

Please enter "biostructure" as the verification code.

PGAM1 Protein Crystal

(CBCRY11)  Download Datasheet
Background
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 Da
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
Gene ID
5223
Chromosome Location
10q25.3
Function
bisphosphoglycerate 2-phosphatase activity; bisphosphoglycerate mutase activity; hydrolase activity; isomerase activity; phosphoglycerate mutase activity; protein kinase binding
Reference
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