2IXD

Crystal structure of the putative deacetylase BC1534 from Bacillus cereus

2IXD の概要

• エントリーDOI: 10.2210/pdb2ixd/pdb
• 分子名称: LMBE-RELATED PROTEIN, ZINC ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: hexamer, deacetylase, rossmann fold, zinc-dependent metalloenzyme, hydrolase
• 由来する生物種: BACILLUS CEREUS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 54761.67

構造登録者

Fadouloglou, V.E.,Bouriotis, V.,Kokkinidis, M. (登録日: 2006-07-07, 公開日: 2007-07-17, 最終更新日: 2023-12-13)

主引用文献

Fadouloglou, V.E.,Deli, A.,Glykos, N.M.,Psylinakis, E.,Bouriotis, V.,Kokkinidis, M.
Crystal Structure of the Bczbp, a Zinc-Binding Protein from Bacillus Cereus
FEBS J., 274:3044-, 2007

PubMed Abstract: 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.

PubMed: 17501983
DOI: 10.1111/J.1742-4658.2007.05834.X

実験手法

X-RAY DIFFRACTION (1.8 Å)