Structural basis of mitochondrial membrane bending by the I-II-III₂-IV₂ supercomplex.

ABSTRACT: Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane¹. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contribute

SUBMITTER: Muhleip A 

PROVIDER: S-EPMC10060162 | biostudies-literature | 2023 Mar

REPOSITORIES: biostudies-literature