5PGM

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

Summary for 5PGM

• Entry DOI: 10.2210/pdb5pgm/pdb
• Descriptor: PHOSPHOGLYCERATE MUTASE 1, SULFATE ION, ALANINE, ... (4 entities in total)
• Functional Keywords: isomerase, transferase (phosphoryl), glycolytic enzyme
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 8
• Total formula weight: 221765.05

Authors

Rigden, D.J.,Phillips, S.E.V.,Fothergill-Gilmore, L.A. (deposition date: 1998-08-19, release date: 1999-02-16, Last modification date: 2024-12-25)

Primary citation

Rigden, D.J.,Walter, R.A.,Phillips, S.E.,Fothergill-Gilmore, L.A.
Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism.
J.Mol.Biol., 286:1507-1517, 1999

PubMed Abstract: The structure of a new crystal form of Saccharomyces cerevisiae phosphoglycerate mutase has been solved and refined to 2.12 A with working and free R-factors of 19.7 and 22.9 %, respectively. Higher-resolution data and greater non-crystallographic symmetry have produced a more accurate protein structure than previously. Prominent among the differences from the previous structure is the presence of two sulphate ions within each active site cleft. The separation of the sulphates suggests that they may occupy the same sites as phospho groups of the bisphosphate ligands of the enzyme. Plausible binding modes for 2,3-bisphosphoglycerate and 1, 3-bisphosphoglycerate are thereby suggested. These results support previous conclusions from mutant studies, highlight interesting new targets for mutagenesis and suggest a possible mechanism of enzyme phosphorylation.

PubMed: 10064712
DOI: 10.1006/jmbi.1999.2566

Experimental method

X-RAY DIFFRACTION (2.12 Å)