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1e59
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 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/ | + | 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]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11884145 11884145] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11884145 11884145] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| + | [[Category: Phosphoglycerate mutase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bond, C.S.]] | [[Category: Bond, C.S.]] | ||
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[[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 10:51:13 2007'' |
Revision as of 08:46, 30 October 2007
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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 10:51:13 2007
