7TCH
BceAB E169Q variant ATP-bound conformation
7TCH の概要
| エントリーDOI | 10.2210/pdb7tch/pdb |
| EMDBエントリー | 25811 25812 |
| 分子名称 | Bacitracin export permease protein BceB, Bacitracin export ATP-binding protein BceA, 4-amino-4-deoxy-1-O-[(S)-hydroxy{[(2E,6E,10Z,14Z,18Z,22E,26E,30E)-3,7,11,15,19,23,27,31,35-nonamethylhexatriaconta-2,6,10,14,18,22,26,30,34-nonaen-1-yl]oxy}phosphoryl]-alpha-L-arabinopyranose, ... (4 entities in total) |
| 機能のキーワード | bceab, bacitracin, transporter, transport protein |
| 由来する生物種 | Bacillus subtilis subsp. subtilis str. 168 詳細 |
| タンパク質・核酸の鎖数 | 3 |
| 化学式量合計 | 132613.43 |
| 構造登録者 | |
| 主引用文献 | George, N.L.,Schilmiller, A.L.,Orlando, B.J. Conformational snapshots of the bacitracin sensing and resistance transporter BceAB. Proc.Natl.Acad.Sci.USA, 119:e2123268119-e2123268119, 2022 Cited by PubMed Abstract: SignificanceMany gram-positive organisms have evolved an elegant solution to sense and resist antimicrobial peptides that inhibit cell-wall synthesis. These organisms express an unusual "Bce-type" adenosine triphosphate-binding cassette (ABC) transporter that recognizes complexes formed between antimicrobial peptides and lipids involved in cell-wall biosynthesis. In this work, we provide the first structural snapshots of a Bce-type ABC transporter trapped in different conformational states. Our structures and associated biochemical data provide key insights into the novel target protection mechanism that these unusual ABC transporters use to sense and resist antimicrobial peptides. The studies described herein set the stage to begin developing a comprehensive molecular understanding of the diverse interactions between antimicrobial peptides and conserved resistance machinery found across most gram-positive organisms. PubMed: 35349335DOI: 10.1073/pnas.2123268119 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.7 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






