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7TGH

Cryo-EM structure of respiratory super-complex CI+III2 from Tetrahymena thermophila

This is a non-PDB format compatible entry.
Summary for 7TGH
Entry DOI10.2210/pdb7tgh/pdb
EMDB information25882
DescriptorNADH-ubiquinone oxidoreductase chain 1, Rieske iron-sulfur protein, ubiquinol-cytochrome C reductase iron-sulfur subunit, Ubiquinol-cytochrome C reductase hinge protein, ... (94 entities in total)
Functional Keywordsmitochondrial respiration, electron transport chain, oxidoreductase, super-complex ci+iii2, membrane protein
Biological sourceTetrahymena thermophila
More
Total number of polymer chains91
Total formula weight2416171.59
Authors
Zhou, L.,Maldonado, M.,Padavannil, A.,Guo, F.,Letts, J.A. (deposition date: 2022-01-07, release date: 2022-04-06, Last modification date: 2024-12-25)
Primary citationZhou, L.,Maldonado, M.,Padavannil, A.,Guo, F.,Letts, J.A.
Structures of Tetrahymena 's respiratory chain reveal the diversity of eukaryotic core metabolism.
Science, 376:831-839, 2022
Cited by
PubMed Abstract: Respiration is a core biological energy-converting process whose last steps are carried out by a chain of multisubunit complexes in the inner mitochondrial membrane. To probe the functional and structural diversity of eukaryotic respiration, we examined the respiratory chain of the ciliate (Tt). Using cryo-electron microscopy on a mixed sample, we solved structures of a supercomplex between Tt complex I (Tt-CI) and Tt-CIII (Tt-SC I+III) and a structure of Tt-CIV. Tt-SC I+III (~2.3 megadaltons) is a curved assembly with structural and functional symmetry breaking. Tt-CIV is a ~2.7-megadalton dimer with more than 50 subunits per protomer, including mitochondrial carriers and a TIM8-TIM13-like domain. Our structural and functional study of the respiratory chain reveals divergence in key components of eukaryotic respiration, thereby expanding our understanding of core metabolism.
PubMed: 35357889
DOI: 10.1126/science.abn7747
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.6 Å)
Structure validation

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