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Moe A, Kovalova T, Król S, Yanofsky DJ, Bott M, Sjöstrand D, Rubinstein JL, Högbom M, Brzezinski P
Structure 30 (3) 338-349.e3 [2022-03-03; online 2021-12-14]
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 CIII2CIV2 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 CIII2 dimer flanked by a CIV on two sides. A menaquinone is bound in each of the QN and QP sites in each CIII and an additional menaquinone is positioned ∼14 Å from heme bL. 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 bL. 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
Crossref 10.1016/j.str.2021.11.008
pii: S0969-2126(21)00420-2