3I13

Bacillus cereus Zn-dependent metallo-beta-lactamase at pH 5.8

3I13 の概要

• エントリーDOI: 10.2210/pdb3i13/pdb
• 関連するPDBエントリー: 1bc2 1bvt 3I0V 3I11 3I14 3I15
• 分子名称: Beta-lactamase 2, ZINC ION (3 entities in total)
• 機能のキーワード: antibiotic resistance, metallo-beta-lactamase superfamily, zn-dependent hydrolase, hydrolase, metal-binding
• 由来する生物種: Bacillus cereus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25126.35

構造登録者

Gonzalez, J.M.,Buschiazzo, A.,Vila, A.J. (登録日: 2009-06-25, 公開日: 2009-12-29, 最終更新日: 2024-02-21)

主引用文献

Gonzalez, J.M.,Buschiazzo, A.,Vila, A.J.
Evidence of adaptability in metal coordination geometry and active-site loop conformation among B1 metallo-beta-lactamases .
Biochemistry, 49:7930-7938, 2010

PubMed Abstract: Subclass B1 beta-lactamases are Zn(II)-dependent hydrolases that confer bacterial resistance to most clinically useful beta-lactam antibiotics. The enzyme BcII from Bacillus cereus is a prototypical enzyme that belongs to this group, the first Zn(II)-dependent beta-lactamase to be discovered. Crucial aspects of the BcII catalytic mechanism and metal binding mode have been assessed mostly on the Co(II)-substituted surrogate. Here we report a high-resolution structure of Co(II)-BcII, revealing a metal coordination geometry identical to that of the native zinc enzyme. In addition, a high-resolution structure of the apoenzyme, together with structures with different degrees of metal occupancy and oxidation levels of a conserved Cys ligand, discloses a considerable mobility of two loops containing four metal ligands (namely, regions His116-Arg121 and Gly219-Cys221). This flexibility is expected to assist in the structural rearrangement of the metal sites during catalytic turnover, which, along with the coordination geometry adaptability of Zn(II) ions, grants the interaction with a variety of substrates, a characteristic feature of B1 metallo-beta-lactamases.

PubMed: 20677753
DOI: 10.1021/bi100894r

実験手法

X-RAY DIFFRACTION (1.74 Å)