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-Structure paper
Title | Cryo-EM structures of engineered active bc-cbb type CIIICIV super-complexes and electronic communication between the complexes. |
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Journal, issue, pages | Nat Commun, Vol. 12, Issue 1, Page 929, Year 2021 |
Publish date | Feb 10, 2021 |
Authors | Stefan Steimle / Trevor van Eeuwen / Yavuz Ozturk / Hee Jong Kim / Merav Braitbard / Nur Selamoglu / Benjamin A Garcia / Dina Schneidman-Duhovny / Kenji Murakami / Fevzi Daldal / |
PubMed Abstract | Respiratory electron transport complexes are organized as individual entities or combined as large supercomplexes (SC). Gram-negative bacteria deploy a mitochondrial-like cytochrome (cyt) bc (Complex ...Respiratory electron transport complexes are organized as individual entities or combined as large supercomplexes (SC). Gram-negative bacteria deploy a mitochondrial-like cytochrome (cyt) bc (Complex III, CIII), and may have specific cbb-type cyt c oxidases (Complex IV, CIV) instead of the canonical aa-type CIV. Electron transfer between these complexes is mediated by soluble (c) and membrane-anchored (c) cyts. Here, we report the structure of an engineered bc-cbb type SC (CIIICIV, 5.2 Å resolution) and three conformers of native CIII (3.3 Å resolution). The SC is active in vivo and in vitro, contains all catalytic subunits and cofactors, and two extra transmembrane helices attributed to cyt c and the assembly factor CcoH. The cyt c is integral to SC, its cyt domain is mobile and it conveys electrons to CIV differently than cyt c. The successful production of a native-like functional SC and determination of its structure illustrate the characteristics of membrane-confined and membrane-external respiratory electron transport pathways in Gram-negative bacteria. |
External links | Nat Commun / PubMed:33568648 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 - 7.2 Å |
Structure data | EMDB-22189, PDB-6xi0: EMDB-22224, PDB-6xkt: EMDB-22225, PDB-6xku: EMDB-22226, PDB-6xkv: EMDB-22227, PDB-6xkw: EMDB-22228, PDB-6xkx: EMDB-22230, PDB-6xkz: |
Chemicals | ChemComp-FES: ChemComp-HEC: ChemComp-CU: |
Source |
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Keywords | OXIDOREDUCTASE / cytochrome bc1 membrane protein complex ubiquinone:cytochrome c oxidoreductase Complex III / TRANSLOCASE/Oxidoreductase / cytochrome bc1 / membrane protein complex / ubiquinone:cytochrome c oxidoreductase / Complex III / TRANSLOCASE-Oxidoreductase complex / cbb3-COX / Complex IV |