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Structure paper

TitleCryo-EM structures of engineered active bc-cbb type CIIICIV super-complexes and electronic communication between the complexes.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 929, Year 2021
Publish dateFeb 10, 2021
AuthorsStefan Steimle / Trevor van Eeuwen / Yavuz Ozturk / Hee Jong Kim / Merav Braitbard / Nur Selamoglu / Benjamin A Garcia / Dina Schneidman-Duhovny / Kenji Murakami / Fevzi Daldal /
PubMed AbstractRespiratory 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 linksNat Commun / PubMed:33568648 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 7.2 Å
Structure data

22189

6xi0

EMDB-22189, PDB-6xi0:
R. capsulatus cyt bc1 (CIII2) at 3.3A
Method: EM (single particle) / Resolution: 3.3 Å

22224

6xkt

EMDB-22224, PDB-6xkt:
R. capsulatus cyt bc1 with both FeS proteins in c position (CIII2 c-c)
Method: EM (single particle) / Resolution: 3.75 Å

22225

6xku

EMDB-22225, PDB-6xku:
R. capsulatus cyt bc1 with one FeS protein in b position and one in c position (CIII2 b-c)
Method: EM (single particle) / Resolution: 4.2 Å

22226

6xkv

EMDB-22226, PDB-6xkv:
R. capsulatus cyt bc1 with both FeS proteins in b position (CIII2 b-b)
Method: EM (single particle) / Resolution: 3.5 Å

22227

6xkw

EMDB-22227, PDB-6xkw:
R. capsulatus CIII2CIV bipartite super-complex (SC-2A) with CcoH/cy
Method: EM (single particle) / Resolution: 5.2 Å

22228

6xkx

EMDB-22228, PDB-6xkx:
R. capsulatus CIII2CIV tripartite super-complex, conformation A (SC-1A)
Method: EM (single particle) / Resolution: 6.1 Å

22230

6xkz

EMDB-22230, PDB-6xkz:
R. capsulatus CIII2CIV tripartite super-complex, conformation B (SC-1B)
Method: EM (single particle) / Resolution: 7.2 Å

Chemicals

ChemComp-FES:
FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster

ChemComp-HEC:
HEME C / Heme C

ChemComp-CU:
COPPER (II) ION / Copper

Source
  • Rhodobacter capsulatus SB 1003 (bacteria)
  • rhodobacter capsulatus (strain atcc baa-309 / nbrc 16581 / sb1003) (bacteria)
KeywordsOXIDOREDUCTASE / 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

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