2A3M
Structure of Desulfovibrio desulfuricans G20 tetraheme cytochrome (oxidized form)
Summary for 2A3M
| Entry DOI | 10.2210/pdb2a3m/pdb |
| Descriptor | COG3005: Nitrate/TMAO reductases, membrane-bound tetraheme cytochrome c subunit, HEME C (3 entities in total) |
| Functional Keywords | desulfovibrio, tetraheme cytochrome, cytochrome c3, electron transport |
| Biological source | Desulfovibrio desulfuricans subsp. desulfuricans str. |
| Total number of polymer chains | 1 |
| Total formula weight | 16647.53 |
| Authors | Pattarkine, M.V.,Tanner, J.J.,Bottoms, C.A.,Lee, Y.H.,Wall, J.D. (deposition date: 2005-06-25, release date: 2006-04-25, Last modification date: 2024-11-06) |
| Primary citation | Pattarkine, M.V.,Tanner, J.J.,Bottoms, C.A.,Lee, Y.H.,Wall, J.D. Desulfovibrio desulfuricans G20 Tetraheme Cytochrome Structure at 1.5A and Cytochrome Interaction with Metal Complexes J.Mol.Biol., 358:1314-1327, 2006 Cited by PubMed Abstract: The structure of the type I tetraheme cytochrome c(3) from Desulfovibrio desulfuricans G20 was determined to 1.5 Angstrom by X-ray crystallography. In addition to the oxidized form, the structure of the molybdate-bound form of the protein was determined from oxidized crystals soaked in sodium molybdate. Only small structural shifts were obtained with metal binding, consistent with the remarkable structural stability of this protein. In vitro experiments with pure cytochrome showed that molybdate could oxidize the reduced cytochrome, although not as rapidly as U(VI) present as uranyl acetate. Alterations in the overall conformation and thermostability of the metal-oxidized protein were investigated by circular dichroism studies. Again, only small changes in protein structure were documented. The location of the molybdate ion near heme IV in the crystal structure suggested heme IV as the site of electron exit from the reduced cytochrome and implicated Lys14 and Lys56 in binding. Analysis of structurally conserved water molecules in type I cytochrome c(3) crystal structures identified interactions predicted to be important for protein stability and possibly for intramolecular electron transfer among heme molecules. PubMed: 16580681DOI: 10.1016/j.jmb.2006.03.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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