Structures of AAA protein translocase Bcs1 suggest translocation mechanism of a folded protein.
ATPases Associated with Diverse Cellular Activities
/ chemistry
Adenosine Diphosphate
/ metabolism
Adenosine Triphosphate
/ metabolism
Animals
Crystallography, X-Ray
Mice
Mitochondrial Proteins
/ chemistry
Models, Molecular
Molecular Chaperones
/ chemistry
Protein Conformation
Protein Domains
Protein Folding
Protein Multimerization
Protein Transport
Journal
Nature structural & molecular biology
ISSN: 1545-9985
Titre abrégé: Nat Struct Mol Biol
Pays: United States
ID NLM: 101186374
Informations de publication
Date de publication:
02 2020
02 2020
Historique:
received:
02
10
2019
accepted:
07
01
2020
entrez:
12
2
2020
pubmed:
12
2
2020
medline:
21
4
2020
Statut:
ppublish
Résumé
The mitochondrial membrane-bound AAA protein Bcs1 translocate substrates across the mitochondrial inner membrane without previous unfolding. One substrate of Bcs1 is the iron-sulfur protein (ISP), a subunit of the respiratory Complex III. How Bcs1 translocates ISP across the membrane is unknown. Here we report structures of mouse Bcs1 in two different conformations, representing three nucleotide states. The apo and ADP-bound structures reveal a homo-heptamer and show a large putative substrate-binding cavity accessible to the matrix space. ATP binding drives a contraction of the cavity by concerted motion of the ATPase domains, which could push substrate across the membrane. Our findings shed light on the potential mechanism of translocating folded proteins across a membrane, offer insights into the assembly process of Complex III and allow mapping of human disease-associated mutations onto the Bcs1 structure.
Identifiants
pubmed: 32042153
doi: 10.1038/s41594-020-0373-0
pii: 10.1038/s41594-020-0373-0
pmc: PMC8482623
mid: NIHMS1731262
doi:
Substances chimiques
BCS1L protein, mouse
0
Mitochondrial Proteins
0
Molecular Chaperones
0
Adenosine Diphosphate
61D2G4IYVH
Adenosine Triphosphate
8L70Q75FXE
ATPases Associated with Diverse Cellular Activities
EC 3.6.4.-
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
202-209Subventions
Organisme : Intramural NIH HHS
ID : ZIA BC010600
Pays : United States
Organisme : Intramural NIH HHS
ID : ZIC ES103326
Pays : United States
Commentaires et corrections
Type : CommentIn
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