4NQ2

Structure of Zn(II)-bound metallo-beta-lactamse VIM-2 from Pseudomonas aeruginosa

4NQ2 の概要

• エントリーDOI: 10.2210/pdb4nq2/pdb
• 関連するPDBエントリー: 1ko2 1ko3 2yz3
• 分子名称: Beta-lactamase class B VIM-2, ZINC ION, ACETATE ION, ... (4 entities in total)
• 機能のキーワード: metallo-beta-lactamase, hydrolase, zinc binding
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28095.50

構造登録者

Aitha, M.,Nix, J.C.,Crowder, M.W.,Page, R.C. (登録日: 2013-11-23, 公開日: 2014-11-12, 最終更新日: 2023-09-20)

主引用文献

Aitha, M.,Marts, A.R.,Bergstrom, A.,Moller, A.J.,Moritz, L.,Turner, L.,Nix, J.C.,Bonomo, R.A.,Page, R.C.,Tierney, D.L.,Crowder, M.W.
Biochemical, Mechanistic, and Spectroscopic Characterization of Metallo-beta-lactamase VIM-2.
Biochemistry, 53:7321-7331, 2014

PubMed Abstract: This study examines metal binding to metallo-β-lactamase VIM-2, demonstrating the first successful preparation of a Co(II)-substituted VIM-2 analogue. Spectroscopic studies of the half- and fully metal loaded enzymes show that both Zn(II) and Co(II) bind cooperatively, where the major species present, regardless of stoichiometry, are apo- and di-Zn (or di-Co) enzymes. We determined the di-Zn VIM-2 structure to a resolution of 1.55 Å, and this structure supports results from spectroscopic studies. Kinetics, both steady-state and pre-steady-state, show that VIM-2 utilizes a mechanism that proceeds through a very short-lived anionic intermediate when chromacef is used as the substrate. Comparison with other B1 enzymes shows that those that bind Zn(II) cooperatively are better poised to protonate the intermediate on its formation, compared to those that bind Zn(II) non-cooperatively, which uniformly build up substantial amounts of the intermediate.

PubMed: 25356958
DOI: 10.1021/bi500916y

実験手法

X-RAY DIFFRACTION (1.55 Å)