3KNS
Bacillus cereus metallo-beta-lactamase Cys221Asp mutant, 20 mM Zn(II)
3KNS の概要
エントリーDOI | 10.2210/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: 22729148DOI: 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) |
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