5DM7

Crystal structure of the 50S ribosomal subunit from Deinococcus radiodurans in complex with hygromycin A

5DM7 の概要

• エントリーDOI: 10.2210/pdb5dm7/pdb
• 分子名称: 50S ribosomal protein L1, 50S ribosomal protein L15, 50S ribosomal protein L16, ... (32 entities in total)
• 機能のキーワード: protein synthesis, peptidyltransferase, antibiotic, aminocyclitol, ribosome
• 由来する生物種: Deinococcus radiodurans; 詳細
• タンパク質・核酸の鎖数: 30
• 化学式量合計: 1360557.41

構造登録者

Kaminishi, T.,Schedlbauer, A.,Ochoa-Lizarralde, B.,Connell, S.R.,Fucini, P. (登録日: 2015-09-08, 公開日: 2015-11-11, 最終更新日: 2024-11-20)

主引用文献

Kaminishi, T.,Schedlbauer, A.,Fabbretti, A.,Brandi, L.,Ochoa-Lizarralde, B.,He, C.G.,Milon, P.,Connell, S.R.,Gualerzi, C.O.,Fucini, P.
Crystallographic characterization of the ribosomal binding site and molecular mechanism of action of Hygromycin A.
Nucleic Acids Res., 43:10015-10025, 2015

PubMed Abstract: Hygromycin A (HygA) binds to the large ribosomal subunit and inhibits its peptidyl transferase (PT) activity. The presented structural and biochemical data indicate that HygA does not interfere with the initial binding of aminoacyl-tRNA to the A site, but prevents its subsequent adjustment such that it fails to act as a substrate in the PT reaction. Structurally we demonstrate that HygA binds within the peptidyl transferase center (PTC) and induces a unique conformation. Specifically in its ribosomal binding site HygA would overlap and clash with aminoacyl-A76 ribose moiety and, therefore, its primary mode of action involves sterically restricting access of the incoming aminoacyl-tRNA to the PTC.

PubMed: 26464437
DOI: 10.1093/nar/gkv975

実験手法

X-RAY DIFFRACTION (3 Å)