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1vm1

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(New page: 200px<br /><applet load="1vm1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vm1, resolution 2.02&Aring;" /> '''STRUCTURE OF SHV-1 B...)
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Revision as of 20:41, 24 November 2007

Image:1vm1.gif

1vm1, resolution 2.02Å

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STRUCTURE OF SHV-1 BETA-LACTAMASE INHIBITED BY TAZOBACTAM

Overview

Two species resulting from the reaction of the SHV-1 class A, beta-lactamase with the sulfone inhibitor tazobactam have been trapped at, 100 K and mapped by X-ray crystallography at 2.0 A resolution. An acyclic, form of tazobactam is covalently bonded to the catalytic Ser70 side chain, and a second species, a five-atom vinyl carboxylic acid fragment of, tazobactam, is bonded to Ser130. It is proposed that the electron density, map of the crystal is a composite picture of two complexes, each with only, a single bound species. It is estimated that the two complexes exist in, the crystal in approximately equal populations. Results are discussed in, relation to the mechanism-based inhibition of class A beta-lactamases by, the similar inhibitors sulbactam and clavulanic acid.

About this Structure

1VM1 is a Single protein structure of sequence from Klebsiella pneumoniae with MA4, TBE, AKR and TAZ as ligands. This structure superseeds the now removed PDB entry 1G56. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.

Reference

Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam., Kuzin AP, Nukaga M, Nukaga Y, Hujer A, Bonomo RA, Knox JR, Biochemistry. 2001 Feb 13;40(6):1861-6. PMID:11327849

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