1xpb
From Proteopedia
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Revision as of 14:27, 30 October 2007
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STRUCTURE OF BETA-LACTAMASE TEM1
Overview
beta-Lactamases are bacterial enzymes which catalyse the hydrolysis of the, beta-lactam ring of penicillins, cephalosporins and related compounds, thus inactivating these antibiotics. The crystal structure of the TEM1, beta-lactamase has been determined at 1.9 A resolution by the, molecular-replacement method, using the atomic coordinates of two, homologous beta-lactamase refined structures which show about 36% strict, identity in their amino-acid sequences and 1.96 A r.m.s. deviation between, equivalent Calpha atoms. The TEM1 enzyme crystallizes in space group, P2(1)2(1)2(1) and there is one molecule per asymmetric unit. The structure, was refined by simulated annealing to an R-factor of 15.6% for 15 086, reflections with I >/= 2sigma(I) in the resolution range 5.0-1.9 A. The, final ... [(full description)]
About this Structure
1XPB is a [Single protein] structure of sequence from [Escherichia coli] with SO4 as [ligand]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: ACT. Full crystallographic information is available from [OCA].
Reference
TEM1 beta-lactamase structure solved by molecular replacement and refined structure of the S235A mutant., Fonze E, Charlier P, To'th Y, Vermeire M, Raquet X, Dubus A, Frere JM, Acta Crystallogr D Biol Crystallogr. 1995 Sep 1;51(Pt 5):682-94. PMID:15299797
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