5pgm
From Proteopedia
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| - | [[Image:5pgm.gif|left|200px]]<br /><applet load="5pgm" size=" | + | [[Image:5pgm.gif|left|200px]]<br /><applet load="5pgm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="5pgm, resolution 2.12Å" /> | caption="5pgm, resolution 2.12Å" /> | ||
'''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE'''<br /> | '''SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 5PGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with SO4 and ALA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Known structural/functional Sites: <scene name='pdbsite=CIA:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CIA</scene>, <scene name='pdbsite=CIB:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CIB</scene>, <scene name='pdbsite=CIC:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CIC</scene>, <scene name='pdbsite=CID:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CID</scene>, <scene name='pdbsite=CIE:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CIE</scene>, <scene name='pdbsite=CIF:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CIF</scene>, <scene name='pdbsite=CIG:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CIG</scene> and <scene name='pdbsite=CIH:Catalytic Site. HIS 8 Phosphorylation Is Required To Pri ...'>CIH</scene>. Full crystallographic information is available from [http:// | + | 5PGM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=ALA:'>ALA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Phosphoglycerate_mutase Phosphoglycerate mutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.2.1 5.4.2.1] Known structural/functional Sites: <scene name='pdbsite=CIA:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CIA</scene>, <scene name='pdbsite=CIB:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CIB</scene>, <scene name='pdbsite=CIC:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CIC</scene>, <scene name='pdbsite=CID:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CID</scene>, <scene name='pdbsite=CIE:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CIE</scene>, <scene name='pdbsite=CIF:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CIF</scene>, <scene name='pdbsite=CIG:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CIG</scene> and <scene name='pdbsite=CIH:Catalytic+Site.+HIS+8+Phosphorylation+Is+Required+To+Pri+...'>CIH</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5PGM OCA]. |
==Reference== | ==Reference== | ||
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[[Category: transferase (phosphoryl)]] | [[Category: transferase (phosphoryl)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:53:31 2008'' |
Revision as of 08:53, 3 February 2008
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SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE
Overview
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.
About this Structure
5PGM is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Active as Phosphoglycerate mutase, with EC number 5.4.2.1 Known structural/functional Sites: , , , , , , and . 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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