Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Elongational stalling activates mitoribosome-associated quality control.
Journal, issue, pages	Science, Vol. 370, Issue 6520, Page 1105-1110, Year 2020
Publish date	Nov 27, 2020
Authors	Nirupa Desai / Hanting Yang / Viswanathan Chandrasekaran / Razina Kazi / Michal Minczuk / V Ramakrishnan /
PubMed Abstract	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 ...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.
External links	Science / PubMed:33243891 / PubMed Central
Methods	EM (single particle)
Resolution	3.1 - 4.4 Å
Structure data	EMDB-11636: Cryo-EM structure of the human mitoribosome in the rotated-1 state with A/A and P/E mt-tRNAs Method: EM (single particle) / Resolution: 3.9 Å EMDB-11637: Cryo-EM structure of Oxa1L-bound human mitoribosomal large subunit Method: EM (single particle) / Resolution: 3.1 Å 11641 7a5f EMDB-11641, PDB-7a5f: Structure of the stalled human mitoribosome with P- and E-site mt-tRNAs Method: EM (single particle) / Resolution: 4.4 Å 11642 7a5g EMDB-11642, PDB-7a5g: Structure of the elongating human mitoribosome bound to mtEF-Tu.GMPPCP and A/T mt-tRNA Method: EM (single particle) / Resolution: 4.33 Å 11643 7a5h EMDB-11643, PDB-7a5h: Structure of the split human mitoribosomal large subunit with rescue factors mtRF-R and MTRES1 Method: EM (single particle) / Resolution: 3.3 Å 11644 7a5i EMDB-11644, PDB-7a5i: Structure of the human mitoribosome with A- P-and E-site mt-tRNAs Method: EM (single particle) / Resolution: 3.7 Å 11645 7a5j EMDB-11645, PDB-7a5j: Structure of the split human mitoribosomal large subunit with P-and E-site mt-tRNAs Method: EM (single particle) / Resolution: 3.1 Å 11646 7a5k EMDB-11646, PDB-7a5k: Structure of the human mitoribosome in the post translocation state bound to mtEF-G1 Method: EM (single particle) / Resolution: 3.7 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-ZN: Unknown entry ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying moleculeYM / Guanosine diphosphate ChemComp-SO4: SULFATE ION / Sulfate ChemComp-MLI: MALONATE ION / Malonic acid ChemComp-CL: Unknown entry / Chloride ChemComp-NA: Unknown entry ChemComp-HOH: WATER / Water ChemComp-SPD: SPERMIDINE / Spermidine ChemComp-GCP: PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-PCP, energy-carrying molecule analogueYM ChemComp-PNS: 4'-PHOSPHOPANTETHEINE / Phosphopantetheine
Source	homo sapiens (human) thermus thermophilus (strain hb27 / atcc baa-163 / dsm 7039) (bacteria) human (human) thermus thermophilus hb27 (bacteria)
Keywords	RIBOSOME / mitochondrial ribosome / ribosome stalling / cryo-EM