3MK7
The structure of CBB3 cytochrome oxidase
Summary for 3MK7
| Entry DOI | 10.2210/pdb3mk7/pdb |
| Descriptor | Cytochrome c oxidase, cbb3-type, subunit N, HEME C, HEXACYANOFERRATE(3-), ... (11 entities in total) |
| Functional Keywords | tm helices, oxidoreductase |
| Biological source | Pseudomonas stutzeri More |
| Total number of polymer chains | 16 |
| Total formula weight | 462028.28 |
| Authors | Buschmann, S.,Warkentin, E.,Michel, H.,Ermler, U. (deposition date: 2010-04-14, release date: 2010-08-04, Last modification date: 2024-11-06) |
| Primary citation | Buschmann, S.,Warkentin, E.,Xie, H.,Langer, J.D.,Ermler, U.,Michel, H. The Structure of cbb3 Cytochrome Oxidase Provides Insights into Proton Pumping Science, 329:327-330, 2010 Cited by PubMed Abstract: The heme-copper oxidases (HCOs) accomplish the key event of aerobic respiration; they couple O2 reduction and transmembrane proton pumping. To gain new insights into the still enigmatic process, we structurally characterized a C-family HCO--essential for the pathogenicity of many bacteria--that differs from the two other HCO families, A and B, that have been structurally analyzed. The x-ray structure of the C-family cbb3 oxidase from Pseudomonas stutzeri at 3.2 angstrom resolution shows an electron supply system different from families A and B. Like family-B HCOs, C HCOs have only one pathway, which conducts protons via an alternative tyrosine-histidine cross-link. Structural differences around hemes b and b3 suggest a different redox-driven proton-pumping mechanism and provide clues to explain the higher activity of family-C HCOs at low oxygen concentrations. PubMed: 20576851DOI: 10.1126/science.1187303 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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