6XKU
R. capsulatus cyt bc1 with one FeS protein in b position and one in c position (CIII2 b-c)
Summary for 6XKU
| Entry DOI | 10.2210/pdb6xku/pdb |
| Related | 6XI0 |
| EMDB information | 22225 |
| Descriptor | Ubiquinol-cytochrome c reductase iron-sulfur subunit, Cytochrome b, Cytochrome c1, ... (5 entities in total) |
| Functional Keywords | cytochrome bc1, membrane protein complex, ubiquinone:cytochrome c oxidoreductase, complex iii, oxidoreductase, translocase-oxidoreductase complex, translocase/oxidoreductase |
| Biological source | Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003) More |
| Total number of polymer chains | 6 |
| Total formula weight | 204471.04 |
| Authors | Steimle, S.,Van Eeuwen, T.,Ozturk, Y.,Kim, H.J.,Braitbard, M.,Selamoglu, N.,Garcia, B.A.,Schneidman-Duhovny, D.,Murakami, K.,Daldal, F. (deposition date: 2020-06-27, release date: 2020-12-30, Last modification date: 2021-03-03) |
| Primary citation | Steimle, S.,van Eeuwen, T.,Ozturk, Y.,Kim, H.J.,Braitbard, M.,Selamoglu, N.,Garcia, B.A.,Schneidman-Duhovny, D.,Murakami, K.,Daldal, F. Cryo-EM structures of engineered active bc 1 -cbb 3 type CIII 2 CIV super-complexes and electronic communication between the complexes. Nat Commun, 12:929-929, 2021 Cited by 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 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. PubMed: 33568648DOI: 10.1038/s41467-021-21051-4 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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