2gc0: Difference between revisions

Revision as of 05:37, 29 July 2008

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File:2gc0.png

Template:STRUCTURE 2gc0

The crystal structure of phosphoglucose isomerase from Pyrococcus furiosus in complex with 5-phospho-D-arabinonohydroxamate and zincThe crystal structure of phosphoglucose isomerase from Pyrococcus furiosus in complex with 5-phospho-D-arabinonohydroxamate and zinc

Template:ABSTRACT PUBMED 16580686

About this StructureAbout this Structure

2GC0 is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.

ReferenceReference

Evidence supporting a cis-enediol-based mechanism for Pyrococcus furiosus phosphoglucose isomerase., Berrisford JM, Hounslow AM, Akerboom J, Hagen WR, Brouns SJ, van der Oost J, Murray IA, Michael Blackburn G, Waltho JP, Rice DW, Baker PJ, J Mol Biol. 2006 May 19;358(5):1353-66. Epub 2006 Mar 24. PMID:16580686

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_2gc0|  PDB=2gc0  |  SCENE=  }}
-'''The crystal structure of phosphoglucose isomerase from Pyrococcus furiosus in complex with 5-phospho-D-arabinonohydroxamate and zinc'''
+===The crystal structure of phosphoglucose isomerase from Pyrococcus furiosus in complex with 5-phospho-D-arabinonohydroxamate and zinc===
-==Overview==
+<!--
-The enzymatic aldose ketose isomerisation of glucose and fructose sugars involves the transfer of a hydrogen between their C1 and C2 carbon atoms and, in principle, can proceed through either a direct hydride shift or via a cis-enediol intermediate. Pyrococcus furiosus phosphoglucose isomerase (PfPGI), an archaeal metalloenzyme, which catalyses the interconversion of glucose 6-phosphate and fructose 6-phosphate, has been suggested to operate via a hydride shift mechanism. In contrast, the structurally distinct PGIs of eukaryotic or bacterial origin are thought to catalyse isomerisation via a cis-enediol intermediate. We have shown by NMR that hydrogen exchange between substrate and solvent occurs during the reaction catalysed by PfPGI eliminating the possibility of a hydride-shift-based mechanism. In addition, kinetic measurements on this enzyme have shown that 5-phospho-d-arabinonohydroxamate, a stable analogue of the putative cis-enediol intermediate, is the most potent inhibitor of the enzyme yet discovered. Furthermore, determination and analysis of crystal structures of PfPGI with bound zinc and the substrate F6P, and with a number of competitive inhibitors, and EPR analysis of the coordination of the metal ion within PfPGI, have suggested that a cis-enediol intermediate-based mechanism is used by PfPGI with Glu97 acting as the catalytic base responsible for isomerisation.
+The line below this paragraph, {{ABSTRACT_PUBMED_16580686}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16580686 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16580686}}
 ==About this Structure==
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 [[Category: Cupin]]
 [[Category: Phosphoglucose isomerase]]
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