2ixd
From Proteopedia
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==Overview== | ==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 ... | + | 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 BcZBP nor the biochemical pathway have been conclusively, identified. Here, we present the crystal structure of BcZBP at 1.8 A, resolution. The N-terminal part of the 234 amino acid protein adopts a, Rossmann fold whereas the C-terminal part consists of two beta-strands and, two alpha-helices. In the crystal, the protein forms a compact hexamer, in, agreement with solution data. A zinc binding site and a potential active, site have been identified in each monomer. These sites have extensive, similarities to those found in two known zinc-dependent hydrolases with, deacetylase activity, MshB and LpxC, despite a low degree of amino acid, sequence identity. The functional implications and a possible catalytic, mechanism are discussed. |
==About this Structure== | ==About this Structure== | ||
| - | 2IXD is a | + | 2IXD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus] with ZN and ACT as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IXD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-dependent metalloenzyme]] | [[Category: zinc-dependent metalloenzyme]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:20:45 2007'' |
Revision as of 12:15, 5 November 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 BcZBP nor the biochemical pathway have been conclusively, identified. Here, we present the crystal structure of BcZBP at 1.8 A, resolution. The N-terminal part of the 234 amino acid protein adopts a, Rossmann fold whereas the C-terminal part consists of two beta-strands and, two alpha-helices. In the crystal, the protein forms a compact hexamer, in, agreement with solution data. A zinc binding site and a potential active, site have been identified in each monomer. These sites have extensive, similarities to those found in two known zinc-dependent hydrolases with, deacetylase activity, MshB and LpxC, despite a low degree of amino acid, sequence identity. The functional implications and a possible catalytic, mechanism are discussed.
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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