Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex.
Science
; 373(6561): 1377-1381, 2021 Sep 17.
Article
in En
| MEDLINE
| ID: mdl-34446444
ABSTRACT
ß barrel outer membrane proteins (ß-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and assembly machinery (SAM) mediate the assembly of ß-OMPs. We investigated the SAM-mediated assembly of the translocase of the outer membrane (TOM) core complex. Cryoelectron microscopy structures of SAMfully folded Tom40 and the SAM-Tom40/Tom5/Tom6 complexes at ~3-angstrom resolution reveal that Sam37 stabilizes the mature Tom40 mainly through electrostatic interactions, thus facilitating subsequent TOM assembly. These results support the ß barrel switching model and provide structural insights into the assembly and release of ß barrel complexes.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carrier Proteins
/
Mitochondrial Membrane Transport Proteins
/
Multiprotein Complexes
/
Mitochondrial Membranes
Limits:
Humans
Language:
En
Journal:
Science
Year:
2021
Document type:
Article
Affiliation country: