3G4S

Co-crystal structure of Tiamulin bound to the large ribosomal subunit

3G4S の概要

• エントリーDOI: 10.2210/pdb3g4s/pdb
• 関連するPDBエントリー: 3G6E 3G71
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L11P, 50S ribosomal protein L13P, ... (39 entities in total)
• 機能のキーワード: large ribosomal subunit, tiamulin, haloarcula marismortui, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, metal-binding, zinc-finger, ribosome
• 由来する生物種: Haloarcula 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: 1461536.52

構造登録者

Gurel, G.,Blaha, G.,Moore, P.B.,Steitz, T.A. (登録日: 2009-02-04, 公開日: 2009-04-28, 最終更新日: 2023-09-06)

主引用文献

Gurel, G.,Blaha, G.,Moore, P.B.,Steitz, T.A.
U2504 determines the species specificity of the A-site cleft antibiotics: the structures of tiamulin, homoharringtonine, and bruceantin bound to the ribosome.
J.Mol.Biol., 389:146-156, 2009

PubMed Abstract: Structures have been obtained for the complexes that tiamulin, homoharringtonine, and bruceantin form with the large ribosomal subunit of Haloarcula marismortui at resolutions ranging from 2.65 to 3.2 A. They show that all these inhibitors block protein synthesis by competing with the amino acid side chains of incoming aminoacyl-tRNAs for binding in the A-site cleft in the peptidyl-transferase center, which is universally conserved. In addition, these structures support the hypothesis that the species specificity exhibited by the A-site cleft inhibitors is determined by the interactions they make, or fail to make, with a single nucleotide, U2504 (Escherichia coli). In the ribosome, the position of U2504 is controlled by its interactions with neighboring nucleotides, whose identities vary among kingdoms.

PubMed: 19362093
DOI: 10.1016/j.jmb.2009.04.005

実験手法

X-RAY DIFFRACTION (3.2 Å)