2BPN
SOLUTION STRUCTURE OF DESULFOVIBRIO VULGARIS (HILDENBOROUGH) FERRICYTOCHROME C3, NMR, 20 STRUCTURES
Summary for 2BPN
| Entry DOI | 10.2210/pdb2bpn/pdb |
| Related | 1A2I 1GX7 1MDV 2CTH 2CYM |
| NMR Information | BMRB: 5625 |
| Descriptor | CYTOCHROME C3, HEME C (2 entities in total) |
| Functional Keywords | electron transport, hemeprotein, cytochrome c3, redox cooperativity, redox-bohr cooperativity, transduction, paramagnetic |
| Biological source | DESULFOVIBRIO VULGARIS |
| Cellular location | Periplasm: P00131 |
| Total number of polymer chains | 1 |
| Total formula weight | 14161.48 |
| Authors | Messias, A.C.,Aguiar, A.P.,Brennan, L.,Xavier, A.V.,Turner, D.L. (deposition date: 2005-04-21, release date: 2006-03-15, Last modification date: 2024-10-09) |
| Primary citation | Messias, A.C.,Aguiar, A.P.,Brennan, L.,Salgueiro, C.A.,Saraiva, L.M.,Xavier, A.V.,Turner, D.L. Solution Structures of Tetrahaem Ferricytochrome C(3) from Desulfovibrio Vulgaris (Hildenborough) and its K45Q Mutant: The Molecular Basis of Cooperativity. Biochim.Biophys.Acta, 1757:143-, 2006 Cited by PubMed Abstract: The NMR structure of the oxidised wild-type cytochrome c3 from Desulfovibrio vulgaris Hildenborough was determined in solution. Using a newly developed methodology, NMR data from the K45Q mutant was then grafted onto data from the wild-type protein to determine the structure in the region of the mutation. The structural origins of the redox-Bohr effect and haem-haem cooperativities are discussed with respect to the redox-related conformational changes observed in solution. PubMed: 16527248DOI: 10.1016/J.BBABIO.2006.01.007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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