1OND

THE CRYSTAL STRUCTURE OF THE 50S LARGE RIBOSOMAL SUBUNIT FROM DEINOCOCCUS RADIODURANS COMPLEXED WITH TROLEANDOMYCIN MACROLIDE ANTIBIOTIC

1OND の概要

• エントリーDOI: 10.2210/pdb1ond/pdb
• 関連するPDBエントリー: 1JZX 1JZY 1JZZ 1NJM 1NJN 1NKW
• 分子名称: 23S RIBOSOMAL RNA, 50S ribosomal protein L22, 50S ribosomal protein L32, ... (4 entities in total)
• 機能のキーワード: ribosomes, trna, macrolide, antibiotic, exit-tunnel l22, blockage, ribosome
• 由来する生物種: Deinococcus radiodurans; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 956219.85

構造登録者

Berisio, R.,Schluenzen, F.,Harms, J.,Bashan, A.,Auerbach, T.,Baram, D.,Yonath, A. (登録日: 2003-02-27, 公開日: 2003-04-15, 最終更新日: 2023-08-16)

主引用文献

Berisio, R.,Schluenzen, F.,Harms, J.,Bashan, A.,Auerbach, T.,Baram, D.,Yonath, A.
Structural insight into the role of the ribosomal tunnel in cellular regulation
Nat.Struct.Biol., 10:366-370, 2003

PubMed Abstract: Nascent proteins emerge out of ribosomes through an exit tunnel, which was assumed to be a firmly built passive path. Recent biochemical results, however, indicate that the tunnel plays an active role in sequence-specific gating of nascent chains and in responding to cellular signals. Consistently, modulation of the tunnel shape, caused by the binding of the semi-synthetic macrolide troleandomycin to the large ribosomal subunit from Deinococcus radiodurans, was revealed crystallographically. The results provide insights into the tunnel dynamics at high resolution. Here we show that, in addition to the typical steric blockage of the ribosomal tunnel by macrolides, troleandomycin induces a conformational rearrangement in a wall constituent, protein L22, flipping the tip of its highly conserved beta-hairpin across the tunnel. On the basis of mutations that alleviate elongation arrest, the tunnel motion could be correlated with sequence discrimination and gating, suggesting that specific arrest motifs within nascent chain sequences may induce a similar gating mechanism.

PubMed: 12665853
DOI: 10.1038/nsb915

実験手法

X-RAY DIFFRACTION (3.4 Å)