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1qxy
From Proteopedia
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(New page: 200px<br /><applet load="1qxy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qxy, resolution 1.04Å" /> '''Crystal structure of...)
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Revision as of 22:59, 20 November 2007
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Crystal structure of S. aureus methionine aminopeptidase in complex with a ketoheterocycle 618
Overview
High-resolution crystal structures of Staphylococcus aureus methionine, aminopeptidase I in complex with various keto heterocycles and, aminoketones were determined, and the intermolecular ligand interactions, with the enzyme are reported. The compounds are effective inhibitors of, the S. aureus enzyme because of the formation of an uncleavable, tetrahedral intermediate upon binding. The electron densities, unequivocally show the enzyme-catalyzed transition-state analogue, mimicking that for amide bond hydrolysis of substrates.
About this Structure
1QXY is a Single protein structure of sequence from Staphylococcus aureus with CO, ACT and M2C as ligands. Active as Methionyl aminopeptidase, with EC number 3.4.11.18 Full crystallographic information is available from OCA.
Reference
Crystal structures of Staphylococcusaureus methionine aminopeptidase complexed with keto heterocycle and aminoketone inhibitors reveal the formation of a tetrahedral intermediate., Douangamath A, Dale GE, D'Arcy A, Almstetter M, Eckl R, Frutos-Hoener A, Henkel B, Illgen K, Nerdinger S, Schulz H, Mac Sweeney A, Thormann M, Treml A, Pierau S, Wadman S, Oefner C, J Med Chem. 2004 Mar 11;47(6):1325-8. PMID:14998322
Page seeded by OCA on Wed Nov 21 01:06:29 2007
