EMD-14796

Single-particle
2.83 Å
EMD-14796 Deposition: 19/04/2022
Map released: 30/11/2022
Last modified: 13/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-14796

CryoEM structure of mitochondrial complex I from Chaetomium thermophilum (state 2) - membrane arm

EMD-14796

Single-particle
2.83 Å
EMD-14796 Deposition: 19/04/2022
Map released: 30/11/2022
Last modified: 13/11/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Chaetomium thermophilum var. thermophilum DSM 1495
Sample: Mitochondrial NADH:ubiquinone oxidoreductase in LMNG
Fitted models: 7zme (Avg. Q-score: 0.596)

Deposition Authors: Laube E , Kuehlbrandt W
Conformational changes in mitochondrial complex I of the thermophilic eukaryote Chaetomium thermophilum.
Laube E , Meier-Credo J , Langer JD , Kuhlbrandt W
(2022) Sci Adv , 8 , eadc9952 - eadc9952
PUBMED: 36427319
DOI: doi:10.1126/sciadv.adc9952
ISSN: 2375-2548
Abstract:
Mitochondrial complex I is a redox-driven proton pump that generates proton-motive force across the inner mitochondrial membrane, powering oxidative phosphorylation and ATP synthesis in eukaryotes. We report the structure of complex I from the thermophilic fungus Chaetomium thermophilum, determined by cryoEM up to 2.4-Å resolution. We show that the complex undergoes a transition between two conformations, which we refer to as state 1 and state 2. The conformational switch is manifest in a twisting movement of the peripheral arm relative to the membrane arm, but most notably in substantial rearrangements of the Q-binding cavity and the E-channel, resulting in a continuous aqueous passage from the E-channel to subunit ND5 at the far end of the membrane arm. The conformational changes in the complex interior resemble those reported for mammalian complex I, suggesting a highly conserved, universal mechanism of coupling electron transport to proton pumping.