5CTM
Structure of BPu1 beta-lactamase
5CTM の概要
| エントリーDOI | 10.2210/pdb5ctm/pdb |
| 関連するPDBエントリー | 5CTN |
| 分子名称 | Beta-lactamase, CITRATE ANION, 1,2-ETHANEDIOL, ... (5 entities in total) |
| 機能のキーワード | hydrolase, beta-lactamase |
| 由来する生物種 | Bacillus pumilus |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 55479.87 |
| 構造登録者 | |
| 主引用文献 | Toth, M.,Antunes, N.T.,Stewart, N.K.,Frase, H.,Bhattacharya, M.,Smith, C.A.,Vakulenko, S.B. Class D beta-lactamases do exist in Gram-positive bacteria. Nat.Chem.Biol., 12:9-14, 2016 Cited by PubMed Abstract: Production of β-lactamases of one of four molecular classes (A, B, C and D) is the major mechanism of bacterial resistance to β-lactams, the largest class of antibiotics, which have saved countless lives since their inception 70 years ago. Although several hundred efficient class D enzymes have been identified in Gram-negative pathogens over the last four decades, none have been reported in Gram-positive bacteria. Here we demonstrate that efficient class D β-lactamases capable of hydrolyzing a wide array of β-lactam substrates are widely disseminated in various species of environmental Gram-positive organisms. Class D enzymes of Gram-positive bacteria have a distinct structural architecture and employ a unique substrate-binding mode that is quite different from that of all currently known class A, C and D β-lactamases. These enzymes thus constitute a previously unknown reservoir of novel antibiotic-resistance enzymes. PubMed: 26551395DOI: 10.1038/nchembio.1950 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1 Å) |
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