High-resolution cryo-EM analysis of the yeast ATP synthase in a lipid membrane.
Science
; 360(6389)2018 05 11.
Article
em En
| MEDLINE
| ID: mdl-29650704
ABSTRACT
Mitochondrial adenosine triphosphate (ATP) synthase comprises a membrane embedded Fo motor that rotates to drive ATP synthesis in the F1 subunit. We used single-particle cryo-electron microscopy (cryo-EM) to obtain structures of the full complex in a lipid bilayer in the absence or presence of the inhibitor oligomycin at 3.6- and 3.8-angstrom resolution, respectively. To limit conformational heterogeneity, we locked the rotor in a single conformation by fusing the F6 subunit of the stator with the δ subunit of the rotor. Assembly of the enzyme with the F6-δ fusion caused a twisting of the rotor and a 9° rotation of the Fo c10-ring in the direction of ATP synthesis, relative to the structure of isolated Fo Our cryo-EM structures show how F1 and Fo are coupled, give insight into the proton translocation pathway, and show how oligomycin blocks ATP synthesis.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Motores Moleculares
/
ATPases Mitocondriais Próton-Translocadoras
/
Proteínas de Saccharomyces cerevisiae
/
Membranas Mitocondriais
Idioma:
En
Revista:
Science
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
Estados Unidos