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8E7S

III2IV2 respiratory supercomplex from Saccharomyces cerevisiae with 4 bound UQ6

Summary for 8E7S
Entry DOI10.2210/pdb8e7s/pdb
EMDB information27940
DescriptorCytochrome b-c1 complex subunit 1, mitochondrial, Cytochrome c oxidase subunit 1, Cytochrome c1, heme protein, mitochondrial, ... (32 entities in total)
Functional Keywordss.cerevisiae, respiratory supercomplex, cardiolipin, uq6, oxidoreductase
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains44
Total formula weight997883.53
Authors
Hryc, C.F.,Mileykovskaya, E.,Baker, M.,Dowhan, W. (deposition date: 2022-08-24, release date: 2023-05-24, Last modification date: 2024-11-13)
Primary citationHryc, C.F.,Mallampalli, V.K.P.S.,Bovshik, E.I.,Azinas, S.,Fan, G.,Serysheva, I.I.,Sparagna, G.C.,Baker, M.L.,Mileykovskaya, E.,Dowhan, W.
Structural insights into cardiolipin replacement by phosphatidylglycerol in a cardiolipin-lacking yeast respiratory supercomplex.
Nat Commun, 14:2783-2783, 2023
Cited by
PubMed Abstract: Cardiolipin is a hallmark phospholipid of mitochondrial membranes. Despite established significance of cardiolipin in supporting respiratory supercomplex organization, a mechanistic understanding of this lipid-protein interaction is still lacking. To address the essential role of cardiolipin in supercomplex organization, we report cryo-EM structures of a wild type supercomplex (IVIIIIV) and a supercomplex (IIIIV) isolated from a cardiolipin-lacking Saccharomyces cerevisiae mutant at 3.2-Å and 3.3-Å resolution, respectively, and demonstrate that phosphatidylglycerol in IIIIV occupies similar positions as cardiolipin in IVIIIIV. Lipid-protein interactions within these complexes differ, which conceivably underlies the reduced level of IVIIIIV and high levels of IIIIV and free III and IV in mutant mitochondria. Here we show that anionic phospholipids interact with positive amino acids and appear to nucleate a phospholipid domain at the interface between the individual complexes, which dampen charge repulsion and further stabilize interaction, respectively, between individual complexes.
PubMed: 37188665
DOI: 10.1038/s41467-023-38441-5
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.2 Å)
Structure validation

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