8BF9
Molecular view of ER membrane remodeling by the Sec61/TRAP translocon.
Summary for 8BF9
| Entry DOI | 10.2210/pdb8bf9/pdb |
| EMDB information | 16017 |
| Descriptor | RNA (1766), Ribosomal protein L23/L25 N-terminal domain-containing protein, RL26 protein (Fragment), ... (19 entities in total) |
| Functional Keywords | membrane protein, protein translocation, protein biogenesis., transport protein |
| Biological source | Ovis aries More |
| Total number of polymer chains | 19 |
| Total formula weight | 1548686.85 |
| Authors | Karki, S.,Javanainen, M.,Tranter, D.,Rehan, S.,Huiskonen, J.,Happonen, L.,Paavilainen, V. (deposition date: 2022-10-24, release date: 2023-11-01, Last modification date: 2024-10-23) |
| Primary citation | Karki, S.,Javanainen, M.,Rehan, S.,Tranter, D.,Kellosalo, J.,Huiskonen, J.T.,Happonen, L.,Paavilainen, V. Molecular view of ER membrane remodeling by the Sec61/TRAP translocon. Embo Rep., 24:e57910-e57910, 2023 Cited by PubMed Abstract: Protein translocation across the endoplasmic reticulum (ER) membrane is an essential step during protein entry into the secretory pathway. The conserved Sec61 protein-conducting channel facilitates polypeptide translocation and coordinates cotranslational polypeptide-processing events. In cells, the majority of Sec61 is stably associated with a heterotetrameric membrane protein complex, the translocon-associated protein complex (TRAP), yet the mechanism by which TRAP assists in polypeptide translocation remains unknown. Here, we present the structure of the core Sec61/TRAP complex bound to a mammalian ribosome by cryogenic electron microscopy (cryo-EM). Ribosome interactions anchor the Sec61/TRAP complex in a conformation that renders the ER membrane locally thinner by significantly curving its lumenal leaflet. We propose that TRAP stabilizes the ribosome exit tunnel to assist nascent polypeptide insertion through Sec61 and provides a ratcheting mechanism into the ER lumen mediated by direct polypeptide interactions. PubMed: 37983950DOI: 10.15252/embr.202357910 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.69 Å) |
Structure validation
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