1GWS
hexadecaheme high molecular weight cytochrome Hmc from Desulfovibrio vulgaris Hildenborough
Summary for 1GWS
| Entry DOI | 10.2210/pdb1gws/pdb |
| Related | 1H29 |
| Descriptor | HIGH-MOLECULAR-WEIGHT CYTOCHROME C, HEME C (3 entities in total) |
| Functional Keywords | electron transport, multiheme cytochrome, sulfate reducing bacteria, periplasmic, heme |
| Biological source | DESULFOVIBRIO VULGARIS |
| Total number of polymer chains | 1 |
| Total formula weight | 68908.79 |
| Authors | Czjzek, M.,Haser, R.,Bruschi, M. (deposition date: 2002-03-25, release date: 2003-02-13, Last modification date: 2024-10-23) |
| Primary citation | Czjzek, M.,Elantak, L.,Zamboni, V.,Morelli, X.,Dolla, A.,Guerlesquin, F.,Bruschi, M. The Crystal Structure of the Hexadaca-Heme Cytochrome Hmc and a Structural Model of its Complex with Cytochrome C3 Structure, 10:1677-, 2002 Cited by PubMed Abstract: Sulfate-reducing bacteria contain a variety of multi-heme c-type cytochromes. The cytochrome of highest molecular weight (Hmc) contains 16 heme groups and is part of a transmembrane complex involved in the sulfate respiration pathway. We present the 2.42 A resolution crystal structure of the Desulfovibrio vulgaris Hildenborough cytochrome Hmc and a structural model of the complex with its physiological electron transfer partner, cytochrome c(3), obtained by NMR restrained soft-docking calculations. The Hmc is composed of three domains, which exist independently in different sulfate-reducing species, namely cytochrome c(3), cytochrome c(7), and Hcc. The complex involves the last heme at the C-terminal region of the V-shaped Hmc and heme 4 of cytochrome c(3), and represents an example for specific cytochrome-cytochrome interaction. PubMed: 12467575DOI: 10.1016/S0969-2126(02)00909-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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