Structures of the human mitochondrial ribosome bound to EF-G1 reveal distinct features of mitochondrial translation elongation.
Amino Acid Sequence
Binding Sites
Cryoelectron Microscopy
HEK293 Cells
Humans
Mitochondria
/ metabolism
Mitochondrial Membranes
/ metabolism
Mitochondrial Proteins
/ chemistry
Models, Molecular
Nucleic Acid Conformation
Peptide Chain Elongation, Translational
Peptide Elongation Factor G
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Protein Conformation, beta-Strand
Protein Interaction Domains and Motifs
RNA, Mitochondrial
/ chemistry
RNA, Transfer
/ chemistry
Recombinant Proteins
/ chemistry
Ribosomal Proteins
/ chemistry
Ribosomes
/ metabolism
Sequence Alignment
Sequence Homology, Amino Acid
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
31 07 2020
31 07 2020
Historique:
received:
13
04
2020
accepted:
15
07
2020
entrez:
2
8
2020
pubmed:
2
8
2020
medline:
10
9
2020
Statut:
epublish
Résumé
The mammalian mitochondrial ribosome (mitoribosome) and its associated translational factors have evolved to accommodate greater participation of proteins in mitochondrial translation. Here we present the 2.68-3.96 Å cryo-EM structures of the human 55S mitoribosome in complex with the human mitochondrial elongation factor G1 (EF-G1
Identifiants
pubmed: 32737313
doi: 10.1038/s41467-020-17715-2
pii: 10.1038/s41467-020-17715-2
pmc: PMC7395135
doi:
Substances chimiques
GFM1 protein, human
0
Mitochondrial Proteins
0
Peptide Elongation Factor G
0
RNA, Mitochondrial
0
Recombinant Proteins
0
Ribosomal Proteins
0
RNA, Transfer
9014-25-9
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
3830Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM103310
Pays : United States
Organisme : NCRR NIH HHS
ID : P41 RR001209
Pays : United States
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