3CP5
Cytochrome c from rhodothermus marinus
3CP5 の概要
| エントリーDOI | 10.2210/pdb3cp5/pdb |
| 分子名称 | Cytochrome c, SULFATE ION, HEME C, ... (4 entities in total) |
| 機能のキーワード | cytochrome c, electron transfer protein, electron transport |
| 由来する生物種 | Rhodothermus marinus (Rhodothermus obamensis) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 14549.30 |
| 構造登録者 | Stelter, M.,Melo, A.,Saraiva, L.,Teixeira, M.,Archer, M. (登録日: 2008-03-31, 公開日: 2008-10-28, 最終更新日: 2024-10-30) |
| 主引用文献 | Stelter, M.,Melo, A.M.,Pereira, M.M.,Gomes, C.M.,Hreggvidsson, G.O.,Hjorleifsdottir, S.,Saraiva, L.M.,Teixeira, M.,Archer, M. A novel type of monoheme cytochrome c: biochemical and structural characterization at 1.23 A resolution of rhodothermus marinus cytochrome c Biochemistry, 47:11953-11963, 2008 Cited by PubMed Abstract: Monoheme cytochromes of the C-type are involved in a large number of electron transfer processes, which play an essential role in multiple pathways, such as respiratory chains, either aerobic or anaerobic, and the photosynthetic electron transport chains. This study reports the biochemical characterization and the crystallographic structure, at 1.23 A resolution, of a monoheme cytochrome c from the thermohalophilic bacterium Rhodothermus marinus. In addition to an alpha-helical core folded around the heme, common for this type of cytochrome, the X-ray structure reveals one unusual alpha-helix and a unique N-terminal extension, which wraps around the back of the molecule. Based on a thorough structural and amino acid sequence comparison, we propose R. marinus cytochrome c as the first characterized member of a new class of C-type cytochromes. PubMed: 18855424DOI: 10.1021/bi800999g 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.24 Å) |
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