8bf9

Molecular view of ER membrane remodeling by the Sec61/TRAP translocon.

spinqualitylabelsall models 8bf9, resolution 2.69Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8bf9 is a 10 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.69Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A6P3TG10_SHEEP Publication Abstract from PubMed 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. Molecular view of ER membrane remodeling by the Sec61/TRAP translocon.,Karki S, Javanainen M, Rehan S, Tranter D, Kellosalo J, Huiskonen JT, Happonen L, Paavilainen V EMBO Rep. 2023 Dec 6;24(12):e57910. doi: 10.15252/embr.202357910. Epub 2023 Nov , 20. PMID:37983950 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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