2J7A
Crystal structure of cytochrome c nitrite reductase NrfHA complex from Desulfovibrio vulgaris
Summary for 2J7A
| Entry DOI | 10.2210/pdb2j7a/pdb |
| Descriptor | CYTOCHROME C NITRITE REDUCTASE NRFA, CYTOCHROME C QUINOL DEHYDROGENASE NRFH, HEME C, ... (7 entities in total) |
| Functional Keywords | quinol dehydrogenase, cytochrome c nitrite reductase, nrfa, nrfh, napc/nirt family, membrane complex, oxidoreductase |
| Biological source | DESULFOVIBRIO VULGARIS More |
| Total number of polymer chains | 18 |
| Total formula weight | 850740.53 |
| Authors | Rodrigues, M.L.,Oliveira, T.F.,Pereira, I.A.C.,Archer, M. (deposition date: 2006-10-06, release date: 2006-12-06, Last modification date: 2024-11-06) |
| Primary citation | Rodrigues, M.L.,Oliveira, T.F.,Pereira, I.A.C.,Archer, M. X-Ray Structure of the Membrane-Bound Cytochrome C Quinol Dehydrogenase Nrfh Reveals Novel Haem Coordination. Embo J., 25:5951-, 2006 Cited by PubMed Abstract: Oxidation of membrane-bound quinol molecules is a central step in the respiratory electron transport chains used by biological cells to generate ATP by oxidative phosphorylation. A novel family of cytochrome c quinol dehydrogenases that play an important role in bacterial respiratory chains was recognised in recent years. Here, we describe the first structure of a cytochrome from this family, NrfH from Desulfovibrio vulgaris, which forms a stable complex with its electron partner, the cytochrome c nitrite reductase NrfA. One NrfH molecule interacts with one NrfA dimer in an asymmetrical manner, forming a large membrane-bound complex with an overall alpha(4)beta(2) quaternary arrangement. The menaquinol-interacting NrfH haem is pentacoordinated, bound by a methionine from the CXXCHXM sequence, with an aspartate residue occupying the distal position. The NrfH haem that transfers electrons to NrfA has a lysine residue from the closest NrfA molecule as distal ligand. A likely menaquinol binding site, containing several conserved and essential residues, is identified. PubMed: 17139260DOI: 10.1038/SJ.EMBOJ.7601439 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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