4V5A

Structure of the Ribosome Recycling Factor bound to the Thermus thermophilus 70S ribosome with mRNA, ASL-Phe and tRNA-fMet

これはPDB形式変換不可エントリーです。

4V5A の概要

• エントリーDOI: 10.2210/pdb4v5a/pdb
• 関連するPDBエントリー: 1FJG 1GIX 1I94 1I95 1I96 1I97 1IBK 1IBL 1IBM 1J5E 1JGO 1JGP 1JGQ 1L1U 1N32 1N33 1N34 1N36 1PNS 1PNX 1XMO 1XMQ 1XNQ 1XNR 1YL4 2B64 2B9M 2B9O 2F4V 2J00 2J02 2UU9 2UUA 2UUB 2UUC 2UXB 2UXC
• 分子名称: 16S ribosomal RNA, 30S RIBOSOMAL PROTEIN S10, 30S RIBOSOMAL PROTEIN S11, ... (58 entities in total)
• 機能のキーワード: ribosomal protein, ribonucleoprotein, trna-binding, rrna-binding, metal-binding, rrf, trna, mrna, ribosome, recycling, protein biosynthesis, rna-binding, zinc-finger, translation
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 112
• 化学式量合計: 4489984.99

構造登録者

Weixlbaumer, A.,Petry, S.,Dunham, C.M.,Selmer, M.,Kelley, A.C.,Ramakrishnan, V. (登録日: 2007-06-28, 公開日: 2014-07-09, 最終更新日: 2024-11-06)

主引用文献

Weixlbaumer, A.,Petry, S.,Dunham, C.M.,Selmer, M.,Kelley, A.C.,Ramakrishnan, V.
Crystal structure of the ribosome recycling factor bound to the ribosome.
Nat. Struct. Mol. Biol., 14:733-737, 2007

PubMed Abstract: In bacteria, disassembly of the ribosome at the end of translation is facilitated by an essential protein factor termed ribosome recycling factor (RRF), which works in concert with elongation factor G. Here we describe the crystal structure of the Thermus thermophilus RRF bound to a 70S ribosomal complex containing a stop codon in the A site, a transfer RNA anticodon stem-loop in the P site and tRNA(fMet) in the E site. The work demonstrates that structures of translation factors bound to 70S ribosomes can be determined at reasonably high resolution. Contrary to earlier reports, we did not observe any RRF-induced changes in bridges connecting the two subunits. This suggests that such changes are not a direct requirement for or consequence of RRF binding but possibly arise from the subsequent stabilization of a hybrid state of the ribosome.

PubMed: 17660830
DOI: 10.1038/nsmb1282

実験手法

X-RAY DIFFRACTION (3.5 Å)