1RWJ
c7-type three-heme cytochrome domain
Summary for 1RWJ
| Entry DOI | 10.2210/pdb1rwj/pdb |
| Related | 1hh5 1os6 |
| Descriptor | Cytochrome c family protein, HEME C (3 entities in total) |
| Functional Keywords | multiheme cytochrome c, cytochrome c7, geobacter sulfurreducens, geobacter metallireducens, heme coordination in c-type cytochromes, electron transport |
| Biological source | Geobacter sulfurreducens |
| Total number of polymer chains | 1 |
| Total formula weight | 10711.78 |
| Authors | Pokkuluri, P.R.,Londer, Y.Y.,Duke, N.E.C.,Erickson, J.,Pessanha, M.,Salgueiro, C.A.,Schiffer, M. (deposition date: 2003-12-16, release date: 2004-08-03, Last modification date: 2024-10-30) |
| Primary citation | Pokkuluri, P.R.,Londer, Y.Y.,Duke, N.E.C.,Erickson, J.,Pessanha, M.,Salgueiro, C.A.,Schiffer, M. Structure of a novel c7-type three-heme cytochrome domain from a multidomain cytochrome c polymer. Protein Sci., 13:1684-1692, 2004 Cited by PubMed Abstract: The structure of a novel c(7)-type cytochrome domain that has two bishistidine coordinated hemes and one heme with histidine, methionine coordination (where the sixth ligand is a methionine residue) was determined at 1.7 A resolution. This domain is a representative of domains that form three polymers encoded by the Geobacter sulfurreducens genome. Two of these polymers consist of four and one protein of nine c(7)-type domains with a total of 12 and 27 hemes, respectively. Four individual domains (termed A, B, C, and D) from one such multiheme cytochrome c (ORF03300) were cloned and expressed in Escherichia coli. The domain C produced diffraction quality crystals from 2.4 M sodium malonate (pH 7). The structure was solved by MAD method and refined to an R-factor of 19.5% and R-free of 21.8%. Unlike the two c(7) molecules with known structures, one from G. sulfurreducens (PpcA) and one from Desulfuromonas acetoxidans where all three hemes are bishistidine coordinated, this domain contains a heme which is coordinated by a methionine and a histidine residue. As a result, the corresponding heme could have a higher potential than the other two hemes. The apparent midpoint reduction potential, E(app), of domain C is -105 mV, 50 mV higher than that of PpcA. PubMed: 15133162DOI: 10.1110/ps.04626204 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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