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Title | The respiratory supercomplex from C. glutamicum. |
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Journal, issue, pages | Structure, Vol. 30, Issue 3, Page 338-349.e3, Year 2022 |
Publish date | Mar 3, 2022 |
Authors | Agnes Moe / Terezia Kovalova / Sylwia Król / David J Yanofsky / Michael Bott / Dan Sjöstrand / John L Rubinstein / Martin Högbom / Peter Brzezinski / |
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, ...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. |
External links | Structure / PubMed:34910901 |
Methods | EM (single particle) |
Resolution | 2.9 Å |
Structure data | EMDB-13777, PDB-7q21: |
Chemicals | ChemComp-CDL: ChemComp-7PH: ChemComp-TRD: ChemComp-9XX: ChemComp-TWT: ChemComp-CU: ChemComp-MG: ChemComp-HAS: ChemComp-CA: ChemComp-FES: ChemComp-MQ9: ChemComp-9YF: ChemComp-PLM: ChemComp-HEM: ChemComp-HEC: |
Source |
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Keywords | ELECTRON TRANSPORT / MEMBRANE PROTEIN / CRYO-EM / RESPIRATORY SUPERCOMPLEX / ACTINOBACTERIA |