5IMR

Structure of ribosome bound to cofactor at 5.7 angstrom resolution

これはPDB形式変換不可エントリーです。

5IMR の概要

• エントリーDOI: 10.2210/pdb5imr/pdb
• 関連するPDBエントリー: 5IMQ
• EMDBエントリー: 6585
• 分子名称: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (57 entities in total)
• 機能のキーワード: ef4/lepa, ribosome, translational gtpase factors, translocation, reverse
• 由来する生物種: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579); 詳細
• タンパク質・核酸の鎖数: 56
• 化学式量合計: 2310421.33

構造登録者

Kumar, V.,Ero, R.,Jian, G.K.,Ahmed, T.,Zhan, Y.,Bhushan, S.,Gao, Y.G. (登録日: 2016-03-06, 公開日: 2016-05-18, 最終更新日: 2024-10-09)

主引用文献

Kumar, V.,Ero, R.,Ahmed, T.,Goh, K.J.,Zhan, Y.,Bhushan, S.,Gao, Y.G.
Structure of the GTP Form of Elongation Factor 4 (EF4) Bound to the Ribosome
J.Biol.Chem., 291:12943-12950, 2016

PubMed Abstract: Elongation factor 4 (EF4) is a member of the family of ribosome-dependent translational GTPase factors, along with elongation factor G and BPI-inducible protein A. Although EF4 is highly conserved in bacterial, mitochondrial, and chloroplast genomes, its exact biological function remains controversial. Here we present the cryo-EM reconstitution of the GTP form of EF4 bound to the ribosome with P and E site tRNAs at 3.8-Å resolution. Interestingly, our structure reveals an unrotated ribosome rather than a clockwise-rotated ribosome, as observed in the presence of EF4-GDP and P site tRNA. In addition, we also observed a counterclockwise-rotated form of the above complex at 5.7-Å resolution. Taken together, our results shed light on the interactions formed between EF4, the ribosome, and the P site tRNA and illuminate the GTPase activation mechanism at previously unresolved detail.

PubMed: 27137929
DOI: 10.1074/jbc.M116.725945

実験手法

ELECTRON MICROSCOPY (5.7 Å)