7a5g

Structure of the elongating human mitoribosome bound to mtEF-Tu.GMPPCP and A/T mt-tRNA

spinqualitylabelsall models 7a5g, resolution 4.33Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7a5g is a 11 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 4.33Å Ligands: CL, GCP, GDP, MG, MLI, NA, SO4, SPD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RM02_HUMAN Publication Abstract from PubMed The human mitochondrial ribosome (mitoribosome) and associated proteins regulate the synthesis of 13 essential subunits of the oxidative phosphorylation complexes. We report the discovery of a mitoribosome-associated quality control pathway that responds to interruptions during elongation, and we present structures at 3.1- to 3.3-angstrom resolution of mitoribosomal large subunits trapped during ribosome rescue. Release factor homolog C12orf65 (mtRF-R) and RNA binding protein C6orf203 (MTRES1) eject the nascent chain and peptidyl transfer RNA (tRNA), respectively, from stalled ribosomes. Recruitment of mitoribosome biogenesis factors to these quality control intermediates suggests additional roles for these factors during mitoribosome rescue. We also report related cryo-electron microscopy structures (3.7 to 4.4 angstrom resolution) of elongating mitoribosomes bound to tRNAs, nascent polypeptides, the guanosine triphosphatase elongation factors mtEF-Tu and mtEF-G1, and the Oxa1L translocase. Elongational stalling activates mitoribosome-associated quality control.,Desai N, Yang H, Chandrasekaran V, Kazi R, Minczuk M, Ramakrishnan V Science. 2020 Nov 27;370(6520):1105-1110. doi: 10.1126/science.abc7782. PMID:33243891 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elongation factor 3D structures Ribosome 3D structures

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