6zsc | pdb_00006zsc

Human mitochondrial ribosome in complex with E-site tRNA

spinqualitylabelsall models 6zsc, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6zsc 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 3.5Å Ligands: 004, DBB, DOL, GTP, MG, MHT, MHU, MHV, MHW, P5P, Y5P, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RM32_HUMAN Publication Abstract from PubMed Translation of mitochondrial messenger RNA (mt-mRNA) is performed by distinct mitoribosomes comprising at least 36 mitochondria-specific proteins. How these mitoribosomal proteins assist in the binding of mt-mRNA and to what extent they are involved in the translocation of transfer RNA (mt-tRNA) is unclear. To visualize the process of translation in human mitochondria, we report ~3.0 A resolution structure of the human mitoribosome, including the L7/L12 stalk, and eight structures of its functional complexes with mt-mRNA, mt-tRNAs, recycling factor and additional trans factors. The study reveals a transacting protein module LRPPRC-SLIRP that delivers mt-mRNA to the mitoribosomal small subunit through a dedicated platform formed by the mitochondria-specific protein mS39. Mitoribosomal proteins of the large subunit mL40, mL48, and mL64 coordinate translocation of mt-tRNA. The comparison between those structures shows dynamic interactions between the mitoribosome and its ligands, suggesting a sequential mechanism of conformational changes. Structural basis of mitochondrial translation.,Aibara S, Singh V, Modelska A, Amunts A Elife. 2020 Aug 19;9. pii: 58362. doi: 10.7554/eLife.58362. PMID:32812867 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ribosome 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA