2ixd
From Proteopedia
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[[Category: zinc-dependent metalloenzyme]] | [[Category: zinc-dependent metalloenzyme]] | ||
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Revision as of 15:13, 30 October 2007
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CRYSTAL STRUCTURE OF THE PUTATIVE DEACETYLASE BC1534 FROM BACILUS CEREUS
Overview
Bacillus cereus is an opportunistic pathogenic bacterium closely related, to Bacillus anthracis, the causative agent of anthrax in mammals. A, significant portion of the B. cereus chromosomal genes are common to B., anthracis, including genes which in B. anthracis code for putative, virulence and surface proteins. B. cereus thus provides a convenient model, organism for studying proteins potentially associated with the, pathogenicity of the highly infectious B. anthracis. The zinc-binding, protein of B. cereus, BcZBP, is encoded from the bc1534 gene which has, three homologues to B. anthracis. The protein exhibits deacetylase, activity with the N-acetyl moiety of the N-acetylglucosamine and the, diacetylchitobiose and triacetylchitotriose. However, neither the specific, substrate of the ... [(full description)]
About this Structure
2IXD is a [Single protein] structure of sequence from [Bacillus cereus] with ZN and ACT as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the BcZBP, a zinc-binding protein from Bacillus cereus., Fadouloglou VE, Deli A, Glykos NM, Psylinakis E, Bouriotis V, Kokkinidis M, FEBS J. 2007 Jun;274(12):3044-54. Epub 2007 May 14. PMID:17501983
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