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3KNS

Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)

3KNS の概要
エントリーDOI10.2210/pdb3kns/pdb
関連するPDBエントリー1bc2 1bvt 3knr
分子名称Beta-lactamase 2, ZINC ION, SULFATE ION, ... (6 entities in total)
機能のキーワードmetallo-beta-lactamase, zn-dependent hydrolase, antibiotic resistance, hydrolase, metal-binding
由来する生物種Bacillus cereus
細胞内の位置Periplasm : P04190
タンパク質・核酸の鎖数4
化学式量合計101762.19
構造登録者
Medrano Martin, F.J.,Gonzalez, J.M.,Vila, A.J. (登録日: 2009-11-12, 公開日: 2010-11-24, 最終更新日: 2024-02-21)
主引用文献Gonzalez, J.M.,Meini, M.R.,Tomatis, P.E.,Medrano Martin, F.J.,Cricco, J.A.,Vila, A.J.
Metallo-beta-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions.
Nat.Chem.Biol., 8:698-700, 2012
Cited by
PubMed Abstract: A number of multiresistant bacterial pathogens inactivate antibiotics by producing Zn(II)-dependent β-lactamases. We show that metal uptake leading to an active dinuclear enzyme in the periplasmic space of Gram-negative bacteria is ensured by a cysteine residue, an unusual metal ligand in oxidizing environments. Kinetic, structural and affinity data show that such Zn(II)-cysteine interaction is an adaptive trait that tunes the metal binding affinity, thus enabling antibiotic resistance at restrictive Zn(II) concentrations.
PubMed: 22729148
DOI: 10.1038/nchembio.1005
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.58 Å)
構造検証レポート
Validation report summary of 3kns
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-06-11に公開中

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