6GIQ

Saccharomyces cerevisiae respiratory supercomplex III2IV

Summary for 6GIQ

• Entry DOI: 10.2210/pdb6giq/pdb
• EMDB information: 0004
• Descriptor: BJ4_G0001550.mRNA.1.CDS.1, BJ4_G0023510.mRNA.1.CDS.1, Cytochrome c oxidase subunit 1, ... (35 entities in total)
• Functional Keywords: respiratory chain, supercomplex, bc1 complex, cytochrome c oxidase, electron transport
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 32
• Total formula weight: 736651.78

Authors

Rathore, S.,Berndtsson, J.,Conrad, J.,Ott, M. (deposition date: 2018-05-15, release date: 2019-01-02, Last modification date: 2024-10-09)

Primary citation

Rathore, S.,Berndtsson, J.,Marin-Buera, L.,Conrad, J.,Carroni, M.,Brzezinski, P.,Ott, M.
Cryo-EM structure of the yeast respiratory supercomplex.
Nat. Struct. Mol. Biol., 26:50-57, 2019

PubMed Abstract: Respiratory chain complexes execute energy conversion by connecting electron transport with proton translocation over the inner mitochondrial membrane to fuel ATP synthesis. Notably, these complexes form multi-enzyme assemblies known as respiratory supercomplexes. Here we used single-particle cryo-EM to determine the structures of the yeast mitochondrial respiratory supercomplexes IIIIV and IIIIV, at 3.2-Å and 3.5-Å resolutions, respectively. We revealed the overall architecture of the supercomplex, which deviates from the previously determined assemblies in mammals; obtained a near-atomic structure of the yeast complex IV; and identified the protein-protein and protein-lipid interactions implicated in supercomplex formation. Take together, our results demonstrate convergent evolution of supercomplexes in mitochondria that, while building similar assemblies, results in substantially different arrangements and structural solutions to support energy conversion.

PubMed: 30598556
DOI: 10.1038/s41594-018-0169-7

Experimental method

ELECTRON MICROSCOPY (3.23 Å)