Structural insight into mitochondrial β-barrel outer membrane protein biogenesis.
Amino Acid Sequence
Cryoelectron Microscopy
Detergents
/ chemistry
Fungal Proteins
/ chemistry
Mitochondria
/ genetics
Mitochondrial Membrane Transport Proteins
/ chemistry
Mitochondrial Membranes
/ metabolism
Multiprotein Complexes
/ chemistry
Protein Biosynthesis
Protein Conformation
Protein Folding
Saccharomyces cerevisiae
/ genetics
Saccharomyces cerevisiae Proteins
/ chemistry
Sequence Homology, Amino Acid
Sordariales
/ genetics
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
03 07 2020
03 07 2020
Historique:
received:
05
03
2020
accepted:
13
06
2020
entrez:
5
7
2020
pubmed:
6
7
2020
medline:
1
9
2020
Statut:
epublish
Résumé
In mitochondria, β-barrel outer membrane proteins mediate protein import, metabolite transport, lipid transport, and biogenesis. The Sorting and Assembly Machinery (SAM) complex consists of three proteins that assemble as a 1:1:1 complex to fold β-barrel proteins and insert them into the mitochondrial outer membrane. We report cryoEM structures of the SAM complex from Myceliophthora thermophila, which show that Sam50 forms a 16-stranded transmembrane β-barrel with a single polypeptide-transport-associated (POTRA) domain extending into the intermembrane space. Sam35 and Sam37 are located on the cytosolic side of the outer membrane, with Sam35 capping Sam50, and Sam37 interacting extensively with Sam35. Sam35 and Sam37 each adopt a GST-like fold, with no functional, structural, or sequence similarity to their bacterial counterparts. Structural analysis shows how the Sam50 β-barrel opens a lateral gate to accommodate its substrates.
Identifiants
pubmed: 32620929
doi: 10.1038/s41467-020-17144-1
pii: 10.1038/s41467-020-17144-1
pmc: PMC7335169
doi:
Substances chimiques
Detergents
0
Fungal Proteins
0
Mitochondrial Membrane Transport Proteins
0
Multiprotein Complexes
0
Saccharomyces cerevisiae Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
3290Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_UU_00015/1
Pays : United Kingdom
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