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CryoEM structure of mitochondrial complex I from Chaetomium thermophilum (inhibited by DDM)CryoEM structure of mitochondrial complex I from Chaetomium thermophilum (inhibited by DDM)
Structural highlights
FunctionPublication Abstract from PubMedMitochondrial 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-A 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. Conformational changes in mitochondrial complex I of the thermophilic eukaryote Chaetomium thermophilum.,Laube E, Meier-Credo J, Langer JD, Kuhlbrandt W Sci Adv. 2022 Nov 25;8(47):eadc9952. doi: 10.1126/sciadv.adc9952. Epub 2022 Nov , 25. PMID:36427319[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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