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8B6F

Cryo-EM structure of NADH:ubiquinone oxidoreductase (complex-I) from respiratory supercomplex of Tetrahymena thermophila

This is a non-PDB format compatible entry.
Summary for 8B6F
Entry DOI10.2210/pdb8b6f/pdb
EMDB information15865
DescriptorLipid-A-disaccharide synthase, Transmembrane protein, putative, NADH dehydrogenase subunit 5, ... (82 entities in total)
Functional Keywordsciliate, mitochondrial, complex-i, supercomplex, electron transport
Biological sourceTetrahymena thermophila SB210
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Total number of polymer chains69
Total formula weight1780503.87
Authors
Muhleip, A.,Kock Flygaard, R.,Amunts, A. (deposition date: 2022-09-27, release date: 2023-03-29, Last modification date: 2024-11-20)
Primary citationMuhleip, A.,Flygaard, R.K.,Baradaran, R.,Haapanen, O.,Gruhl, T.,Tobiasson, V.,Marechal, A.,Sharma, V.,Amunts, A.
Structural basis of mitochondrial membrane bending by the I-II-III 2 -IV 2 supercomplex.
Nature, 615:934-938, 2023
Cited by
PubMed Abstract: Mitochondrial energy conversion requires an intricate architecture of the inner mitochondrial membrane. Here we show that a supercomplex containing all four respiratory chain components contributes to membrane curvature induction in ciliates. We report cryo-electron microscopy and cryo-tomography structures of the supercomplex that comprises 150 different proteins and 311 bound lipids, forming a stable 5.8-MDa assembly. Owing to subunit acquisition and extension, complex I associates with a complex IV dimer, generating a wedge-shaped gap that serves as a binding site for complex II. Together with a tilted complex III dimer association, it results in a curved membrane region. Using molecular dynamics simulations, we demonstrate that the divergent supercomplex actively contributes to the membrane curvature induction and tubulation of cristae. Our findings highlight how the evolution of protein subunits of respiratory complexes has led to the I-II-III-IV supercomplex that contributes to the shaping of the bioenergetic membrane, thereby enabling its functional specialization.
PubMed: 36949187
DOI: 10.1038/s41586-023-05817-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

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