6zm5

Human mitochondrial ribosome in complex with OXA1L, mRNA, A/A tRNA, P/P tRNA and nascent polypeptide

spinqualitylabelsall models 6zm5, resolution 2.89Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zm5 is a 10 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.89Å Ligands: ALA, ATP, AYA, FES, GTP, IAS, K, MG, SAC, THC, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RM19_HUMAN Publication Abstract from PubMed Mitochondrial ribosomes (mitoribosomes) are tethered to the mitochondrial inner membrane to facilitate the cotranslational membrane insertion of the synthesized proteins. We report cryo-electron microscopy structures of human mitoribosomes with nascent polypeptide, bound to the insertase oxidase assembly 1-like (OXA1L) through three distinct contact sites. OXA1L binding is correlated with a series of conformational changes in the mitoribosomal large subunit that catalyze the delivery of newly synthesized polypeptides. The mechanism relies on the folding of mL45 inside the exit tunnel, forming two specific constriction sites that would limit helix formation of the nascent chain. A gap is formed between the exit and the membrane, making the newly synthesized proteins accessible. Our data elucidate the basis by which mitoribosomes interact with the OXA1L insertase to couple protein synthesis and membrane delivery. Mechanism of membrane-tethered mitochondrial protein synthesis.,Itoh Y, Andrell J, Choi A, Richter U, Maiti P, Best RB, Barrientos A, Battersby BJ, Amunts A Science. 2021 Feb 19;371(6531):846-849. doi: 10.1126/science.abe0763. PMID:33602856 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosome 3D structures

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