1e59: Difference between revisions

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.

1E59 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with CL and VO3 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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E59 OCA].  

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