6GZ3

tRNA translocation by the eukaryotic 80S ribosome and the impact of GTP hydrolysis, Translocation-intermediate-POST-1 (TI-POST-1)

これはPDB形式変換不可エントリーです。

6GZ3 の概要

• エントリーDOI: 10.2210/pdb6gz3/pdb
• EMDBエントリー: 0098
• 分子名称: 28S ribosomal RNA, ribosomal protein uS19, ribosomal protein uS9, ... (89 entities in total)
• 機能のキーワード: translocation rabbit ribosome, 80s, eef2, head swivel, rotation, ribosome
• 由来する生物種: Enterobacteria phage SP6; 詳細
• タンパク質・核酸の鎖数: 86
• 化学式量合計: 3326031.43

構造登録者

Flis, J.,Holm, M.,Rundlet, E.J.,Loerke, J.,Hilal, T.,Dabrowski, M.,Buerger, J.,Mielke, T.,Blanchard, S.C.,Spahn, C.M.T.,Budkevich, T.V. (登録日: 2018-07-03, 公開日: 2018-12-05, 最終更新日: 2022-03-30)

主引用文献

Flis, J.,Holm, M.,Rundlet, E.J.,Loerke, J.,Hilal, T.,Dabrowski, M.,Burger, J.,Mielke, T.,Blanchard, S.C.,Spahn, C.M.T.,Budkevich, T.V.
tRNA Translocation by the Eukaryotic 80S Ribosome and the Impact of GTP Hydrolysis.
Cell Rep, 25:2676-2688.e7, 2018

PubMed Abstract: Translocation moves the tRNA⋅mRNA module directionally through the ribosome during the elongation phase of protein synthesis. Although translocation is known to entail large conformational changes within both the ribosome and tRNA substrates, the orchestrated events that ensure the speed and fidelity of this critical aspect of the protein synthesis mechanism have not been fully elucidated. Here, we present three high-resolution structures of intermediates of translocation on the mammalian ribosome where, in contrast to bacteria, ribosomal complexes containing the translocase eEF2 and the complete tRNA⋅mRNA module are trapped by the non-hydrolyzable GTP analog GMPPNP. Consistent with the observed structures, single-molecule imaging revealed that GTP hydrolysis principally facilitates rate-limiting, final steps of translocation, which are required for factor dissociation and which are differentially regulated in bacterial and mammalian systems by the rates of deacyl-tRNA dissociation from the E site.

PubMed: 30517857
DOI: 10.1016/j.celrep.2018.11.040

実験手法

ELECTRON MICROSCOPY (3.6 Å)