4V9H

Crystal structure of the ribosome bound to elongation factor G in the guanosine triphosphatase state

これはPDB形式変換不可エントリーです。

4V9H の概要

• エントリーDOI: 10.2210/pdb4v9h/pdb
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S16, 30S ribosomal protein S17, ... (61 entities in total)
• 機能のキーワード: bacterial proteins, catalysis, models, molecular, peptide elongation factor g, protein biosynthesis, protein conformation, protein structure, tertiary, rna, bacterial, messenger, transfer, ribosomes, thermus thermophilus, ribosome, hybrid state, guanosine triphosphate, guanosine triphosphatase
• 由来する生物種: Thermus thermophilus; 詳細
• 細胞内の位置: Cytoplasm: P80374
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 2306027.96

構造登録者

Tourigny, D.S.,Fernandez, I.S.,Kelley, A.C.,Ramakrishnan, V. (登録日: 2013-03-25, 公開日: 2014-07-09, 最終更新日: 2024-11-27)

主引用文献

Tourigny, D.S.,Fernandez, I.S.,Kelley, A.C.,Ramakrishnan, V.
Elongation factor G bound to the ribosome in an intermediate state of translocation.
Science, 340:1235490-1235490, 2013

PubMed Abstract: A key step of translation by the ribosome is translocation, which involves the movement of messenger RNA (mRNA) and transfer RNA (tRNA) with respect to the ribosome. This allows a new round of protein chain elongation by placing the next mRNA codon in the A site of the 30S subunit. Translocation proceeds through an intermediate state in which the acceptor ends of the tRNAs have moved with respect to the 50S subunit but not the 30S subunit, to form hybrid states. The guanosine triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent movement of mRNA and tRNA with respect to the 30S subunit. Here, we present a crystal structure at 3 angstrom resolution of the Thermus thermophilus ribosome with a tRNA in the hybrid P/E state bound to EF-G with a GTP analog. The structure provides insights into structural changes that facilitate translocation and suggests a common GTPase mechanism for EF-G and elongation factor Tu.

PubMed: 23812720
DOI: 10.1126/science.1235490

実験手法

X-RAY DIFFRACTION (2.857 Å)