6YPU
Acinetobacter baumannii ribosome-amikacin complex - 30S subunit body
6YPU の概要
エントリーDOI | 10.2210/pdb6ypu/pdb |
EMDBエントリー | 10869 |
分子名称 | 16S ribosomal RNA, 30S ribosomal protein S16, 30S ribosomal protein S17, ... (16 entities in total) |
機能のキーワード | antibiotic, amikacin, translation, ribosome |
由来する生物種 | Acinetobacter baumannii (strain ATCC 19606 / DSM 30007 / CIP 70.34 / JCM 6841 / NBRC 109757 / NCIMB 12457 / NCTC 12156 / 81) 詳細 |
タンパク質・核酸の鎖数 | 15 |
化学式量合計 | 1183150.25 |
構造登録者 | Nicholson, D.,Edwards, T.A.,O'Neill, A.J.,Ranson, N.A. (登録日: 2020-04-16, 公開日: 2020-09-16, 最終更新日: 2024-05-22) |
主引用文献 | Nicholson, D.,Edwards, T.A.,O'Neill, A.J.,Ranson, N.A. Structure of the 70S Ribosome from the Human Pathogen Acinetobacter baumannii in Complex with Clinically Relevant Antibiotics. Structure, 28:1087-1100.e3, 2020 Cited by PubMed Abstract: Acinetobacter baumannii is a Gram-negative bacterium primarily associated with hospital-acquired, often multidrug-resistant (MDR) infections. The ribosome-targeting antibiotics amikacin and tigecycline are among the limited arsenal of drugs available for treatment of such infections. We present high-resolution structures of the 70S ribosome from A. baumannii in complex with these antibiotics, as determined by cryoelectron microscopy. Comparison with the ribosomes of other bacteria reveals several unique structural features at functionally important sites, including around the exit of the polypeptide tunnel and the periphery of the subunit interface. The structures also reveal the mode and site of interaction of these drugs with the ribosome. This work paves the way for the design of new inhibitors of translation to address infections caused by MDR A. baumannii. PubMed: 32857965DOI: 10.1016/j.str.2020.08.004 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (2.9 Å) |
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