1e59

From Proteopedia

Revision as of 14:00, 5 November 2007

E.COLI COFACTOR-DEPENDENT PHOSPHOGLYCERATE MUTASE COMPLEXED WITH VANADATE

Overview

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, observed for E.coli dPGM, the inhibited protein's conformation resembles, that of the inactive dephosphorylated Saccharomyces cerevisiae dPGM. The, provision of a high-resolution structure of both active and inactive forms, of dPGM from a single organism, in conjunction with computational, modelling of substrate molecules in the active site provides insight into, the binding of substrates and the specific interactions necessary for, three different activities, mutase, synthase and phosphatase, within a, single active site. The sequence similarity of E.coli and human dPGMs, allows us to correlate structure with clinical pathology.

About 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.

Reference

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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