7ASE
43S preinitiation complex from Trypanosoma cruzi with the kDDX60 helicase
This is a non-PDB format compatible entry.
Summary for 7ASE
| Entry DOI | 10.2210/pdb7ase/pdb |
| EMDB information | 11893 |
| Descriptor | kDDX60, 40S ribosomal protein S18, putative, 40S ribosomal protein S23, putative, ... (55 entities in total) |
| Functional Keywords | preinitiation, factors, kinetoplastid, helicase, translation |
| Biological source | Trypanosoma cruzi More |
| Total number of polymer chains | 52 |
| Total formula weight | 2328334.17 |
| Authors | Bochler, A.,Brito Querido, J.,Prilepskaja, T.,Soufari, H.,Del Cistia, M.L.,Kuhn, L.,Rimoldi Ribeiro, A.,Valasek, L.S.,Hashem, Y. (deposition date: 2020-10-27, release date: 2021-04-14, Last modification date: 2025-12-17) |
| Primary citation | 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 Cited by 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: 33357443DOI: 10.1016/j.celrep.2020.108534 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.33 Å) |
Structure validation
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