5pgm: Difference between revisions

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[[Image:5pgm.~~gif~~|left|200px]]

[[Image:5pgm.png|left|200px]]

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~~'''~~SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE~~'''~~

===SACCHAROMYCES CEREVISIAE PHOSPHOGLYCERATE MUTASE===

~~==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.

The line below this paragraph, {{ABSTRACT_PUBMED_10064712}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10064712 is the PubMed ID number.

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==About this Structure==

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[[Category: Glycolytic enzyme]]

[[Category: Isomerase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sun May~~ ~~4 22~~:37:00 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 14:08:46 2008''

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