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	Stepwise maturation of the peptidyl transferase region of human mitoribosomes.
Journal, issue, pages	Nat Commun, Vol. 12, Issue 1, Page 3671, Year 2021
Publish date	Jun 16, 2021
Authors	Tea Lenarčič / Mateusz Jaskolowski / Marc Leibundgut / Alain Scaiola / Tanja Schönhut / Martin Saurer / Richard G Lee / Oliver Rackham / Aleksandra Filipovska / Nenad Ban /
PubMed Abstract	Mitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes have diverged considerably from the ancestral ...Mitochondrial ribosomes are specialized for the synthesis of membrane proteins responsible for oxidative phosphorylation. Mammalian mitoribosomes have diverged considerably from the ancestral bacterial ribosomes and feature dramatically reduced ribosomal RNAs. The structural basis of the mammalian mitochondrial ribosome assembly is currently not well understood. Here we present eight distinct assembly intermediates of the human large mitoribosomal subunit involving seven assembly factors. We discover that the NSUN4-MTERF4 dimer plays a critical role in the process by stabilizing the 16S rRNA in a conformation that exposes the functionally important regions of rRNA for modification by the MRM2 methyltransferase and quality control interactions with the conserved mitochondrial GTPase MTG2 that contacts the sarcin-ricin loop and the immature active site. The successive action of these factors leads to the formation of the peptidyl transferase active site of the mitoribosome and the folding of the surrounding rRNA regions responsible for interactions with tRNAs and the small ribosomal subunit.
External links	Nat Commun / PubMed:34135320 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.5 Å
Structure data	12845 7odr EMDB-12845, PDB-7odr: State A of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 2.9 Å 12846 7ods EMDB-12846, PDB-7ods: State B of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 3.1 Å 12847 7odt EMDB-12847, PDB-7odt: State C of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 3.1 Å EMDB-12848: State A0 of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 3.1 Å EMDB-12849: State C0 of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 3.5 Å EMDB-12850: State D0' of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 3.3 Å EMDB-12851: State D0'' of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 3.5 Å EMDB-12852: State D of the human mitoribosomal large subunit assembly intermediate Method: EM (single particle) / Resolution: 3.1 Å
Chemicals	ChemComp-PM8: S-(2-{[N-(2-HYDROXY-4-{[HYDROXY(OXIDO)PHOSPHINO]OXY}-3,3-DIMETHYLBUTANOYL)-BETA-ALANYL]AMINO}ETHYL) DECANETHIOATE ChemComp-SAM: S-ADENOSYLMETHIONINE / S-Adenosyl methionine ChemComp-ZN: Unknown entry ChemComp-MG: Unknown entry ChemComp-K: Unknown entry ChemComp-FES: FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster ChemComp-N: ANY 5'-MONOPHOSPHATE NUCLEOTIDE ChemComp-GDP: GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate
Source	homo sapiens (human)
Keywords	RIBOSOME / mitoribosome / assembly intermediate / large subunit / LSU / mt-LSU