3CCS

Structure of Anisomycin resistant 50S Ribosomal Subunit: 23S rRNA mutation G2482A

3CCS の概要

• エントリーDOI: 10.2210/pdb3ccs/pdb
• 関連するPDBエントリー: 3CC2 3CC4 3CC7 3CCE 3CCJ 3CCL 3CCM 3CCQ 3CCR 3CCU 3CCV 3CD6
• 分子名称: 50S ribosomal protein L2P, 50S ribosomal protein L13P, 50S ribosomal protein L14P, ... (38 entities in total)
• 機能のキーワード: g2482a mutation, 23s rrna, large ribosomal subunit, ribosome
• 由来する生物種: Haloarcula marismortui (Halobacterium marismortui); 詳細
• 細胞内の位置: Cytoplasm : P12743
• タンパク質・核酸の鎖数: 31
• 化学式量合計: 1493232.86

構造登録者

Blaha, G.,Gurel, G. (登録日: 2008-02-26, 公開日: 2008-05-20, 最終更新日: 2024-02-21)

主引用文献

Blaha, G.,Gurel, G.,Schroeder, S.J.,Moore, P.B.,Steitz, T.A.
Mutations outside the anisomycin-binding site can make ribosomes drug-resistant.
J.Mol.Biol., 379:505-519, 2008

PubMed Abstract: Eleven mutations that make Haloarcula marismortui resistant to anisomycin, an antibiotic that competes with the amino acid side chains of aminoacyl tRNAs for binding to the A-site cleft of the large ribosomal unit, have been identified in 23S rRNA. The correlation observed between the sensitivity of H. marismortui to anisomycin and the affinity of its large ribosomal subunits for the drug indicates that its response to anisomycin is determined primarily by the binding of the drug to its large ribosomal subunit. The structures of large ribosomal subunits containing resistance mutations show that these mutations can be divided into two classes: (1) those that interfere with specific drug-ribosome interactions and (2) those that stabilize the apo conformation of the A-site cleft of the ribosome relative to its drug-bound conformation. The conformational effects of some mutations of the second kind propagate through the ribosome for considerable distances and are reversed when A-site substrates bind to the ribosome.

PubMed: 18455733
DOI: 10.1016/j.jmb.2008.03.075

実験手法

X-RAY DIFFRACTION (2.95 Å)