7ASK

43S preinitiation complex from Trypanosoma cruzi with the kDDX60 helicase bound with ATP

7ASK の概要

• エントリーDOI: 10.2210/pdb7ask/pdb
• 関連するPDBエントリー: 7ASE
• EMDBエントリー: 11893 11895
• 分子名称: kDDX60, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: preinitiation, factors, kinetoplastid, helicase, translation
• 由来する生物種: Trypanosoma cruzi
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 247201.38

構造登録者

Bochler, A.,Brito Querido, J.,Prilepskaja, T.,Soufari, H.,Del Cistia, M.L.,Kuhn, L.,Rimoldi Ribeiro, A.,Valasek, L.S.,Hashem, Y. (登録日: 2020-10-27, 公開日: 2021-04-14, 最終更新日: 2024-05-01)

主引用文献

Bochler, A.,Querido, J.B.,Prilepskaja, T.,Soufari, H.,Simonetti, A.,Del Cistia, M.L.,Kuhn, L.,Ribeiro, A.R.,Valasek, L.S.,Hashem, Y.
Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts.
Cell Rep, 33:108534-108534, 2020

PubMed Abstract: Canonical mRNA translation in eukaryotes begins with the formation of the 43S pre-initiation complex (PIC). Its assembly requires binding of initiator Met-tRNA and several eukaryotic initiation factors (eIFs) to the small ribosomal subunit (40S). Compared to their mammalian hosts, trypanosomatids present significant structural differences in their 40S, suggesting substantial variability in translation initiation. Here, we determine the structure of the 43S PIC from Trypanosoma cruzi, the parasite causing Chagas disease. Our structure shows numerous specific features, such as the variant eIF3 structure and its unique interactions with the large rRNA expansion segments (ESs) 9, 7, and 6, and the association of a kinetoplastid-specific DDX60-like helicase. It also reveals the 40S-binding site of the eIF5 C-terminal domain and structures of key terminal tails of several conserved eIFs underlying their activities within the PIC. Our results are corroborated by glutathione S-transferase (GST) pull-down assays in both human and T. cruzi and mass spectrometry data.

PubMed: 33357443
DOI: 10.1016/j.celrep.2020.108534

実験手法

ELECTRON MICROSCOPY (4.3 Å)