8EC0
III2IV respiratory supercomplex from Saccharomyces cerevisiae cardiolipin-lacking mutant
Summary for 8EC0
| Entry DOI | 10.2210/pdb8ec0/pdb |
| EMDB information | 28011 |
| Descriptor | Cytochrome b-c1 complex subunit 1, mitochondrial, Cytochrome c1, heme protein, mitochondrial, Cytochrome c oxidase subunit 8, mitochondrial, ... (30 entities in total) |
| Functional Keywords | s.cerevisiae, respiratory supercomplex, phosphatidylglycerol, oxidoreductase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 30 |
| Total formula weight | 735115.04 |
| Authors | Hryc, C.F.,Mileykovskaya, E.,Baker, M.,Dowhan, W. (deposition date: 2022-08-31, release date: 2023-05-24, Last modification date: 2024-11-13) |
| Primary citation | Hryc, 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: 37188665DOI: 10.1038/s41467-023-38441-5 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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