7NFX

Mammalian ribosome nascent chain complex with SRP and SRP receptor in early state A

これはPDB形式変換不可エントリーです。

7NFX の概要

• エントリーDOI: 10.2210/pdb7nfx/pdb
• EMDBエントリー: 12303
• 分子名称: SRP RNA 7SL, uL30, 60S ribosomal protein L7a, ... (59 entities in total)
• 機能のキーワード: signal recognition particle, protein targeting to the er membrane, ribosome
• 由来する生物種: Homo sapiens; 詳細
• タンパク質・核酸の鎖数: 55
• 化学式量合計: 2468070.52

構造登録者

Jomaa, A.,Lee, J.H.,Shan, S.,Ban, N. (登録日: 2021-02-08, 公開日: 2021-06-02, 最終更新日: 2024-05-01)

主引用文献

Lee, J.H.,Jomaa, A.,Chung, S.,Hwang Fu, Y.H.,Qian, R.,Sun, X.,Hsieh, H.H.,Chandrasekar, S.,Bi, X.,Mattei, S.,Boehringer, D.,Weiss, S.,Ban, N.,Shan, S.O.
Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER.
Sci Adv, 7:-, 2021

PubMed Abstract: The conserved signal recognition particle (SRP) cotranslationally delivers ~30% of the proteome to the eukaryotic endoplasmic reticulum (ER). The molecular mechanism by which eukaryotic SRP transitions from cargo recognition in the cytosol to protein translocation at the ER is not understood. Here, structural, biochemical, and single-molecule studies show that this transition requires multiple sequential conformational rearrangements in the targeting complex initiated by guanosine triphosphatase (GTPase)-driven compaction of the SRP receptor (SR). Disruption of these rearrangements, particularly in mutant SRP54 linked to severe congenital neutropenia, uncouples the SRP/SR GTPase cycle from protein translocation. Structures of targeting intermediates reveal the molecular basis of early SRP-SR recognition and emphasize the role of eukaryote-specific elements in regulating targeting. Our results provide a molecular model for the structural and functional transitions of SRP throughout the targeting cycle and show that these transitions provide important points for biological regulation that can be perturbed in genetic diseases.

PubMed: 34020957
DOI: 10.1126/sciadv.abg0942

実験手法

ELECTRON MICROSCOPY (3.2 Å)