1DUW
STRUCTURE OF NONAHEME CYTOCHROME C
Summary for 1DUW
| Entry DOI | 10.2210/pdb1duw/pdb |
| Descriptor | NONAHEME CYTOCHROME C, HEME C, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | heme, electron transport, cytochrome c, hydrogenase, hmc operon |
| Biological source | Desulfovibrio desulfuricans |
| Total number of polymer chains | 1 |
| Total formula weight | 37385.92 |
| Authors | Umhau, S.,Fritz, G.,Diederichs, K.,Breed, J.,Kroneck, P.M.,Welte, W. (deposition date: 2000-01-19, release date: 2001-03-21, Last modification date: 2024-10-30) |
| Primary citation | Umhau, S.,Fritz, G.,Diederichs, K.,Breed, J.,Welte, W.,Kroneck, P.M. Three-dimensional structure of the nonaheme cytochrome c from Desulfovibrio desulfuricans Essex in the Fe(III) state at 1.89 A resolution. Biochemistry, 40:1308-1316, 2001 Cited by PubMed Abstract: A nine heme group containing cytochrome c isolated from the soluble and membrane fractions of Desulfovibrio desulfuricans Essex, termed nonaheme cytochrome c, was crystallized, and the structure was solved using the multiple wavelength anomalous dispersion (MAD) phasing method. Refinement was carried out to a resolution of 1.89 A, and anisotropic temperature factors were addressed to the iron and sulfur atoms in the model. The structure revealed two cytochrome c(3) like domains with the typical arrangement of four heme centers. Both domains flanked an extra heme buried under the protein surface. This heme is held in position by loop extensions in each of the two domains. Although both the N- and C-terminal tetraheme domains exhibit a fold and heme arrangement very similar to that of cytochrome c(3), they differ considerably in their loop extensions and electrostatic surface. Analysis of the structure provides evidence for a different function of both domains, namely, anchoring the protein in a transmembranous complex with the N-terminal domain and formation of an electron-transfer complex with hydrogenase by the C-terminal domain. PubMed: 11170457DOI: 10.1021/bi001479a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.89 Å) |
Structure validation
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