6F0K
Alternative complex III
Summary for 6F0K
| Entry DOI | 10.2210/pdb6f0k/pdb |
| EMDB information | 4165 |
| Descriptor | Cytochrome c family protein, IRON/SULFUR CLUSTER, Fe-S-cluster-containing hydrogenase, ... (10 entities in total) |
| Functional Keywords | electron transfer, quinol oxidation, respiratory chain, membrane protein |
| Biological source | Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10) (Rhodothermus obamensis) More |
| Total number of polymer chains | 7 |
| Total formula weight | 315835.21 |
| Authors | Sousa, J.S.,Calisto, F.,Mills, D.J.,Pereira, M.M.,Vonck, J.,Kuehlbrandt, W. (deposition date: 2017-11-20, release date: 2018-05-09, Last modification date: 2019-12-11) |
| Primary citation | Sousa, J.S.,Calisto, F.,Langer, J.D.,Mills, D.J.,Refojo, P.N.,Teixeira, M.,Kuhlbrandt, W.,Vonck, J.,Pereira, M.M. Structural basis for energy transduction by respiratory alternative complex III. Nat Commun, 9:1728-1728, 2018 Cited by PubMed Abstract: Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump. PubMed: 29712914DOI: 10.1038/s41467-018-04141-8 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.87 Å) |
Structure validation
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