7ZMH

CryoEM structure of mitochondrial complex I from Chaetomium thermophilum (state 1) - membrane arm

Summary for 7ZMH

• Entry DOI: 10.2210/pdb7zmh/pdb
• Related: 7ZM7 7ZM8 7ZMB 7ZME 7ZMG
• EMDB information: 14798
• Descriptor: NADH-ubiquinone oxidoreductase chain 1, NADH-ubiquinone oxidoreductase-like protein, NADH-ubiquinone oxidoreductase chain 4L, ... (32 entities in total)
• Functional Keywords: proton transporter, mitochondrial membrane protein, complex, oxidoreductase
• Biological source: Chaetomium thermophilum var. thermophilum DSM 1495; More
• Total number of polymer chains: 26
• Total formula weight: 731137.30

Authors

Laube, E.,Kuehlbrandt, W. (deposition date: 2022-04-19, release date: 2022-11-30, Last modification date: 2024-10-16)

Primary citation

Laube, E.,Meier-Credo, J.,Langer, J.D.,Kuhlbrandt, W.
Conformational changes in mitochondrial complex I of the thermophilic eukaryote Chaetomium thermophilum.
Sci Adv, 8:eadc9952-eadc9952, 2022

PubMed 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 , 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.

PubMed: 36427319
DOI: 10.1126/sciadv.adc9952

Experimental method

ELECTRON MICROSCOPY (2.47 Å)