1VY4

Crystal structure of the Thermus thermophilus 70S ribosome in the pre-attack state of peptide bond formation containing acylated tRNA-substrates in the A and P sites.

これはPDB形式変換不可エントリーです。

1VY4 の概要

• エントリーDOI: 10.2210/pdb1vy4/pdb
• 分子名称: 16S Ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (61 entities in total)
• 機能のキーワード: 70s, ribosome, translation, peptydil transfer reaction, proton transfer mechanism, acylated trna
• 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: 4551990.81

構造登録者

Polikanov, Y.S.,Steitz, T.A.,Innis, C.A. (登録日: 2014-05-13, 公開日: 2014-08-20, 最終更新日: 2023-12-27)

主引用文献

Polikanov, Y.S.,Steitz, T.A.,Innis, C.A.
A proton wire to couple aminoacyl-tRNA accommodation and peptide-bond formation on the ribosome.
Nat.Struct.Mol.Biol., 21:787-793, 2014

PubMed Abstract: During peptide-bond formation on the ribosome, the α-amine of an aminoacyl-tRNA attacks the ester carbonyl carbon of a peptidyl-tRNA to yield a peptide lengthened by one amino acid. Although the ribosome's contribution to catalysis is predominantly entropic, the lack of high-resolution structural data for the complete active site in complex with full-length ligands has made it difficult to assess how the ribosome might influence the pathway of the reaction. Here, we present crystal structures of preattack and postcatalysis complexes of the Thermus thermophilus 70S ribosome at ~2.6-Å resolution. These structures reveal a network of hydrogen bonds along which proton transfer could take place to ensure the concerted, rate-limiting formation of a tetrahedral intermediate. We propose that, unlike earlier models, the ribosome and the A-site tRNA facilitate the deprotonation of the nucleophile through the activation of a water molecule.

PubMed: 25132179
DOI: 10.1038/nsmb.2871

実験手法

X-RAY DIFFRACTION (2.6 Å)