1bza

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1bza, resolution 1.8Å

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BETA-LACTAMASE TOHO-1 FROM ESCHERICHIA COLI TUH12191

Overview

Bacterial resistance to beta-lactams is mainly due to the production of, beta-lactamase. Especially through the production of extended-spectrum, beta-lactamases (ESBLs), bacteria have acquired resistance not only to, penicillins, but also to expanded-spectrum cephems. Here, we describe the, crystal structure of the E166A mutant of class A beta-lactamase Toho-1 at, 1.8 A resolution, the first reported tertiary structure of an ESBL., Instead of the wild-type enzyme, a mutant Toho-1, in which Glu166 was, replaced with alanine, was used for this study, because of the strong, tendency of the wild-type enzyme to form twinned crystals. The overall, structure of Toho-1 is similar to the crystal structures of non-ESBLs, with no pronounced backbone rearrangement of the framework. However, there, ... [(full description)]

About this Structure

1BZA 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

Crystal structure of the E166A mutant of extended-spectrum beta-lactamase Toho-1 at 1.8 A resolution., Ibuka A, Taguchi A, Ishiguro M, Fushinobu S, Ishii Y, Kamitori S, Okuyama K, Yamaguchi K, Konno M, Matsuzawa H, J Mol Biol. 1999 Feb 5;285(5):2079-87. PMID:9925786

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