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8GZU

Cryo-EM structure of Tetrahymena thermophila respiratory Megacomplex MC (IV2+I+III2+II)2

This is a non-PDB format compatible entry.
Summary for 8GZU
Entry DOI10.2210/pdb8gzu/pdb
EMDB information34403 34404 34405
DescriptorTransmembrane protein, putative, COXTT10, Ymf65, ... (164 entities in total)
Functional Keywordselectron transport chain, supercomplex, membrane protein, tetrahymena thermophila, electron transport
Biological sourceTetrahymena thermophila SB210
More
Total number of polymer chains436
Total formula weight11803642.70
Authors
Wu, M.C.,Hu, Y.Q.,Han, F.Z.,Zhou, L. (deposition date: 2022-09-27, release date: 2023-06-14, Last modification date: 2024-10-16)
Primary citationHan, F.,Hu, Y.,Wu, M.,He, Z.,Tian, H.,Zhou, L.
Structures of Tetrahymena thermophila respiratory megacomplexes on the tubular mitochondrial cristae.
Nat Commun, 14:2542-2542, 2023
Cited by
PubMed Abstract: Tetrahymena thermophila, a classic ciliate model organism, has been shown to possess tubular mitochondrial cristae and highly divergent electron transport chain involving four transmembrane protein complexes (I-IV). Here we report cryo-EM structures of its ~8 MDa megacomplex IV+ (I + III+ II), as well as a ~ 10.6 MDa megacomplex (IV + I + III+ II) at lower resolution. In megacomplex IV+ (I + III+ II), each CIV protomer associates one copy of supercomplex I + III and one copy of CII, forming a half ring-shaped architecture that adapts to the membrane curvature of mitochondrial cristae. Megacomplex (IV+ I + III+ II) defines the relative position between neighbouring half rings and maintains the proximity between CIV and CIII cytochrome c binding sites. Our findings expand the current understanding of divergence in eukaryotic electron transport chain organization and how it is related to mitochondrial morphology.
PubMed: 37248254
DOI: 10.1038/s41467-023-38158-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.18 Å)
Structure validation

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