3JA1

Activation of GTP Hydrolysis in mRNA-tRNA Translocation by Elongation Factor G

これはPDB形式変換不可エントリーです。

3JA1 の概要

• エントリーDOI: 10.2210/pdb3ja1/pdb
• 関連するPDBエントリー: 3J9Z
• EMDBエントリー: 6315 6316
• 分子名称: 30S ribosomal protein S19, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (59 entities in total)
• 機能のキーワード: 70s ribosome, elongation factor g, ef-g, ribosome
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 58
• 化学式量合計: 2311024.77

構造登録者

Li, W.,Liu, Z.,Koripella, R.K.,Langlois, R.,Sanyal, S.,Frank, J. (登録日: 2015-03-30, 公開日: 2015-07-01, 最終更新日: 2024-02-21)

主引用文献

Li, W.,Liu, Z.,Koripella, R.K.,Langlois, R.,Sanyal, S.,Frank, J.
Activation of GTP hydrolysis in mRNA-tRNA translocation by elongation factor G.
Sci Adv, 1:e1500169-e1500169, 2015

PubMed Abstract: During protein synthesis, elongation of the polypeptide chain by each amino acid is followed by a translocation step in which mRNA and transfer RNA (tRNA) are advanced by one codon. This crucial step is catalyzed by elongation factor G (EF-G), a guanosine triphosphatase (GTPase), and accompanied by a rotation between the two ribosomal subunits. A mutant of EF-G, H91A, renders the factor impaired in guanosine triphosphate (GTP) hydrolysis and thereby stabilizes it on the ribosome. We use cryogenic electron microscopy (cryo-EM) at near-atomic resolution to investigate two complexes formed by EF-G H91A in its GTP state with the ribosome, distinguished by the presence or absence of the intersubunit rotation. Comparison of these two structures argues in favor of a direct role of the conserved histidine in the switch II loop of EF-G in GTPase activation, and explains why GTP hydrolysis cannot proceed with EF-G bound to the unrotated form of the ribosome.

PubMed: 26229983
DOI: 10.1126/sciadv.1500169

実験手法

ELECTRON MICROSCOPY (3.6 Å)