8GYM
Cryo-EM structure of Tetrahymena thermophila respiratory mega-complex MC IV2+(I+III2+II)2
This is a non-PDB format compatible entry.
Summary for 8GYM
Entry DOI | 10.2210/pdb8gym/pdb |
EMDB information | 34373 34380 34381 34382 34383 34384 34385 34386 36374 36375 |
Descriptor | Tim10/DDP family zinc finger protein, Transmembrane protein, putative, NADH-ubiquinone oxidoreductase chain 1, ... (171 entities in total) |
Functional Keywords | electron transport chain, supercomplex, membrane protein, tetrahymena thermophila, electron transport |
Biological source | Tetrahymena thermophila SB210 More |
Total number of polymer chains | 326 |
Total formula weight | 9057423.19 |
Authors | |
Primary citation | Han, 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: 37248254DOI: 10.1038/s41467-023-38158-5 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (2.96 Å) |
Structure validation
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