2M5C

Solution Structure of the Bacillus cereus Metallo-Beta-Lactamase BcII

2M5C の概要

• エントリーDOI: 10.2210/pdb2m5c/pdb
• 関連するPDBエントリー: 2M5D
• NMR情報: BMRB: 19047
• 分子名称: Beta-lactamase 2, ZINC ION (2 entities in total)
• 機能のキーワード: bcii, metallo-beta-lactamase, hydrolase
• 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

Karsisiotis, A.I.,Damblon, C.F.,Roberts, G.C.K. (登録日: 2013-02-20, 公開日: 2013-10-09, 最終更新日: 2024-05-15)

主引用文献

Karsisiotis, A.I.,Damblon, C.F.,Roberts, G.C.
Solution structures of the Bacillus cereus metallo-beta-lactamase BcII and its complex with the broad spectrum inhibitor R-thiomandelic acid.
Biochem.J., 456:397-407, 2013

PubMed Abstract: Metallo-β-lactamases, enzymes which inactivate β-lactam antibiotics, are of increasing biological and clinical significance as a source of antibiotic resistance in pathogenic bacteria. In the present study we describe the high-resolution solution NMR structures of the Bacillus cereus metallo-β-lactamase BcII and of its complex with R-thiomandelic acid, a broad-spectrum inhibitor of metallo-β-lactamases. This is the first reported solution structure of any metallo-β-lactamase. There are differences between the solution structure of the free enzyme and previously reported crystal structures in the loops flanking the active site, which are important for substrate and inhibitor binding and catalysis. The binding of R-thiomandelic acid and the roles of active-site residues are defined in detail. Changes in the enzyme structure upon inhibitor binding clarify the role of the mobile β3-β4 loop. Comparisons with other metallo-β-lactamases highlight the roles of individual amino-acid residues in the active site and the β3-β4 loop in inhibitor binding and provide information on the basis of structure-activity relationships among metallo-β-lactamase inhibitors.

PubMed: 24059435
DOI: 10.1042/BJ20131003

実験手法

SOLUTION NMR