5pgm

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SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

Structural highlights

5pgm is a 8 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.12Å
Ligands:ALA, SO4
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PMG1_YEAST Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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.,Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA J Mol Biol. 1999 Mar 12;286(5):1507-17. PMID:10064712[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
2 reviews cite this structure
Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
1 more
18 other articles
No citations found

See Also

References

  1. ↑ Rigden DJ, Walter RA, Phillips SE, Fothergill-Gilmore LA. 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. 1999 Mar 12;286(5):1507-17. PMID:10064712 doi:10.1006/jmbi.1999.2566

Contents


PDB ID 5pgm

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