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7zm7

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CryoEM structure of mitochondrial complex I from Chaetomium thermophilum (inhibited by DDM)

Structural highlights

7zm7 is a 10 chain structure with sequence from Chaetomium thermophilum var. thermophilum DSM 1495. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 2.77Å
Ligands:	, , , , , , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G1DJA6_CHATD

Publication Abstract from PubMed

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-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

↑ Laube E, Meier-Credo J, Langer JD, Kühlbrandt W. Conformational changes in mitochondrial complex I of the thermophilic eukaryote Chaetomium thermophilum. Sci Adv. 2022 Nov 25;8(47):eadc9952. PMID:36427319 doi:10.1126/sciadv.adc9952