The respiratory supercomplex from C. glutamicum

Medientyp: E-Artikel

Titel: The respiratory supercomplex from C. glutamicum

Beteiligte: Moe, Agnes [Verfasser:in]; Kovalova, Terezia [Verfasser:in]; Król, Sylwia [Verfasser:in]; Yanofsky, David J. [Verfasser:in]; Bott, Michael [Verfasser:in]; Sjöstrand, Dan [Verfasser:in]; Rubinstein, John L. [Verfasser:in]; Högbom, Martin [Verfasser:in]; Brzezinski, Peter [Verfasser:in]

Erschienen: Cell Press, 2022

Sprache: Englisch

DOI: https://doi.org/10.1016/j.str.2021.11.008

ISSN: 1878-4186; 0969-2126

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Beschreibung: 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.

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