1e59: Difference between revisions
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E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE COMPLEXED WITH VANADATE
OverviewOverview
The structure of Escherichia coli cofactor-dependent phosphoglycerate, mutase (dPGM), complexed with the potent inhibitor vanadate, has been, determined to a resolution of 1.30 A (R-factor 0.159; R-free 0.213). The, inhibitor is present in the active site, principally as divanadate, but, with evidence of additional vanadate moieties at either end, and, representing a different binding mode to that observed in the structural, homologue prostatic acid phosphatase. The analysis reveals the, enzyme-ligand interactions involved in inhibition of the mutase activity, by vanadate and identifies a water molecule, observed in the native E.coli, dPGM structure which, once activated by vanadate, may dephosphorylate the, active protein. Rather than reflecting the active conformation previously, ... [(full description)]
About this StructureAbout this Structure
1E59 is a [Single protein] structure of sequence from [Escherichia coli] with CL and VO3 as [ligands]. Active as [Phosphoglycerate mutase], with EC number [5.4.2.1]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Mechanistic implications for Escherichia coli cofactor-dependent phosphoglycerate mutase based on the high-resolution crystal structure of a vanadate complex., Bond CS, White MF, Hunter WN, J Mol Biol. 2002 Mar 8;316(5):1071-81. PMID:11884145
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