This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1e59
From Proteopedia
| Line 25: | Line 25: | ||
[[Category: vandate]] | [[Category: vandate]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 15:05:56 2007'' |
Revision as of 13:01, 30 October 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, ... [(full description)]
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
Page seeded by OCA on Tue Oct 30 15:05:56 2007
