5ZLU の概要
エントリーDOI | 10.2210/pdb5zlu/pdb |
EMDBエントリー | 6934 |
分子名称 | RNA (25-mer), 30S ribosomal protein S3, 30S ribosomal protein S4, ... (58 entities in total) |
機能のキーワード | ribosome, antibiotics, macrolides, abc-f protein, azm |
由来する生物種 | Pseudomonas aeruginosa 詳細 |
タンパク質・核酸の鎖数 | 57 |
化学式量合計 | 2280891.92 |
構造登録者 | Su, W.X.,Kumar, V.,Ero, R.,Andrew, S.W.W.,Jian, S.,Yong-Gui, G. (登録日: 2018-03-29, 公開日: 2018-08-01, 最終更新日: 2019-12-04) |
主引用文献 | Su, W.,Kumar, V.,Ding, Y.,Ero, R.,Serra, A.,Lee, B.S.T.,Wong, A.S.W.,Shi, J.,Sze, S.K.,Yang, L.,Gao, Y.G. Ribosome protection by antibiotic resistance ATP-binding cassette protein. Proc. Natl. Acad. Sci. U.S.A., 115:5157-5162, 2018 Cited by PubMed Abstract: The ribosome is one of the richest targets for antibiotics. Unfortunately, antibiotic resistance is an urgent issue in clinical practice. Several ATP-binding cassette family proteins confer resistance to ribosome-targeting antibiotics through a yet unknown mechanism. Among them, MsrE has been implicated in macrolide resistance. Here, we report the cryo-EM structure of ATP form MsrE bound to the ribosome. Unlike previously characterized ribosomal protection proteins, MsrE is shown to bind to ribosomal exit site. Our structure reveals that the domain linker forms a unique needle-like arrangement with two crossed helices connected by an extended loop projecting into the peptidyl-transferase center and the nascent peptide exit tunnel, where numerous antibiotics bind. In combination with biochemical assays, our structure provides insight into how MsrE binding leads to conformational changes, which results in the release of the drug. This mechanism appears to be universal for the ABC-F type ribosome protection proteins. PubMed: 29712846DOI: 10.1073/pnas.1803313115 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.6 Å) |
構造検証レポート
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