7Q21

III2-IV2 respiratory supercomplex from Corynebacterium glutamicum

Summary for 7Q21

• Entry DOI: 10.2210/pdb7q21/pdb
• EMDB information: 13777
• Descriptor: Co-purified unknown transmembrane helices built as polyALA (AscD), Cytochrome bc1 complex cytochrome c subunit, Co-purified unknown peptide built as polyALA (AscE), ... (29 entities in total)
• Functional Keywords: membrane protein, cryo-em, respiratory supercomplex, actinobacteria, electron transport
• Biological source: Corynebacterium glutamicum ATCC 13032; More
• Total number of polymer chains: 26
• Total formula weight: 735451.76

Authors

Kovalova, T.,Moe, A.,Krol, S.,Yanofsky, D.J.,Bott, M.,Sjostrand, D.,Rubinstein, J.L.,Hogbom, M.,Brzezinski, P. (deposition date: 2021-10-22, release date: 2022-02-02, Last modification date: 2024-11-13)

Primary citation

Moe, A.,Kovalova, T.,Krol, S.,Yanofsky, D.J.,Bott, M.,Sjostrand, D.,Rubinstein, J.L.,Hogbom, M.,Brzezinski, P.
The respiratory supercomplex from C. glutamicum.
Structure, 30:338-, 2022

PubMed Abstract: Corynebacterium glutamicum is a preferentially aerobic gram-positive bacterium belonging to the phylum Actinobacteria, which also includes the pathogen Mycobacterium tuberculosis. In these bacteria, respiratory complexes III and IV form a CIIICIV supercomplex that catalyzes oxidation of menaquinol and reduction of dioxygen to water. We isolated the C. glutamicum supercomplex and used cryo-EM to determine its structure at 2.9 Å resolution. The structure shows a central CIII dimer flanked by a CIV on two sides. A menaquinone is bound in each of the Q and Q sites in each CIII and an additional menaquinone is positioned ∼14 Å from heme b. A di-heme cyt. cc subunit electronically connects each CIII with an adjacent CIV, with the Rieske iron-sulfur protein positioned with the iron near heme b. Multiple subunits interact to form a convoluted sub-structure at the cytoplasmic side of the supercomplex, which defines a path for proton transfer into CIV.

PubMed: 34910901
DOI: 10.1016/j.str.2021.11.008

Experimental method

ELECTRON MICROSCOPY (2.9 Å)