2A3M
Structure of Desulfovibrio desulfuricans G20 tetraheme cytochrome (oxidized form)
2A3M の概要
| エントリーDOI | 10.2210/pdb2a3m/pdb |
| 分子名称 | COG3005: Nitrate/TMAO reductases, membrane-bound tetraheme cytochrome c subunit, HEME C (3 entities in total) |
| 機能のキーワード | desulfovibrio, tetraheme cytochrome, cytochrome c3, electron transport |
| 由来する生物種 | Desulfovibrio desulfuricans subsp. desulfuricans str. |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 16647.53 |
| 構造登録者 | Pattarkine, M.V.,Tanner, J.J.,Bottoms, C.A.,Lee, Y.H.,Wall, J.D. (登録日: 2005-06-25, 公開日: 2006-04-25, 最終更新日: 2024-11-06) |
| 主引用文献 | 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 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.5 Å) |
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