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5pgm

From Proteopedia

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[[Image:5pgm.gif|left|200px]]
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{{Seed}}
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[[Image:5pgm.png|left|200px]]
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{{STRUCTURE_5pgm| PDB=5pgm | SCENE= }}
{{STRUCTURE_5pgm| PDB=5pgm | SCENE= }}
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'''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE'''
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===SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 10064712 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10064712}}
==About this Structure==
==About this Structure==
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[[Category: Glycolytic enzyme]]
[[Category: Glycolytic enzyme]]
[[Category: Isomerase]]
[[Category: Isomerase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:37:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:08:46 2008''

Revision as of 11:08, 3 July 2008

Image:5pgm.png

Template:STRUCTURE 5pgm

SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE

Template:ABSTRACT PUBMED 10064712

About this Structure

5PGM is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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

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