4D61

Cryo-EM structures of ribosomal 80S complexes with termination factors and cricket paralysis virus IRES reveal the IRES in the translocated state

4D61 の概要

• エントリーDOI: 10.2210/pdb4d61/pdb
• EMDBエントリー: 2813
• 分子名称: 18S RRNA, 40S RIBOSOMAL PROTEIN S8, 40S RIBOSOMAL PROTEIN S9, ... (37 entities in total)
• 機能のキーワード: crpv ires, ribosome, termination, release factors
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• 細胞内の位置: Cytoplasm: P62495
• タンパク質・核酸の鎖数: 37
• 化学式量合計: 1383135.66

構造登録者

Muhs, M.,Hilal, T.,Mielke, T.,Skabkin, M.A.,Sanbonmatsu, K.Y.,Pestova, T.V.,Spahn, C.M.T. (登録日: 2014-11-07, 公開日: 2015-03-04, 最終更新日: 2017-08-30)

主引用文献

Muhs, M.,Hilal, T.,Mielke, T.,Skabkin, M.A.,Sanbonmatsu, K.Y.,Pestova, T.V.,Spahn, C.M.T.
Cryo-Em of Ribosomal 80S Complexes with Termination Factors Reveals the Translocated Cricket Paralysis Virus Ires.
Mol.Cell, 57:422-, 2015

PubMed Abstract: The cricket paralysis virus (CrPV) uses an internal ribosomal entry site (IRES) to hijack the ribosome. In a remarkable RNA-based mechanism involving neither initiation factor nor initiator tRNA, the CrPV IRES jumpstarts translation in the elongation phase from the ribosomal A site. Here, we present cryoelectron microscopy (cryo-EM) maps of 80S⋅CrPV-STOP ⋅ eRF1 ⋅ eRF3 ⋅ GMPPNP and 80S⋅CrPV-STOP ⋅ eRF1 complexes, revealing a previously unseen binding state of the IRES and directly rationalizing that an eEF2-dependent translocation of the IRES is required to allow the first A-site occupation. During this unusual translocation event, the IRES undergoes a pronounced conformational change to a more stretched conformation. At the same time, our structural analysis provides information about the binding modes of eRF1 ⋅ eRF3 ⋅ GMPPNP and eRF1 in a minimal system. It shows that neither eRF3 nor ABCE1 are required for the active conformation of eRF1 at the intersection between eukaryotic termination and recycling.

PubMed: 25601755
DOI: 10.1016/J.MOLCEL.2014.12.016

実験手法

ELECTRON MICROSCOPY (9 Å)