2CE0
Structure of oxidized Arabidopsis thaliana cytochrome 6A
2CE0 の概要
| エントリーDOI | 10.2210/pdb2ce0/pdb |
| 関連するPDBエントリー | 2CE1 |
| 分子名称 | CYTOCHROME C6, HEME C (3 entities in total) |
| 機能のキーワード | chloroplast, electron transport, heme, iron, thylakoid, photosynthesis, metal-binding, electron transfer |
| 由来する生物種 | ARABIDOPSIS THALIANA (MOUSE EAR CRESS) |
| 細胞内の位置 | Plastid, chloroplast thylakoid lumen (Probable): Q93VA3 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12306.57 |
| 構造登録者 | Marcaida, M.J.,Schlarb-Ridley, B.G.,Worrall, J.A.R.,Wastl, J.,Evans, T.J.,Bendall, D.S.,Luisi, B.F.,Howe, C.J. (登録日: 2006-02-01, 公開日: 2006-07-05, 最終更新日: 2024-11-06) |
| 主引用文献 | Marcaida, M.J.,Schlarb-Ridley, B.G.,Worrall, J.A.R.,Wastl, J.,Evans, T.J.,Bendall, D.S.,Luisi, B.F.,Howe, C.J. Structure of Cytochrome C(6A), a Novel Dithio-Cytochrome of Arabidopsis Thaliana, and its Reactivity with Plastocyanin: Implications for Function. J.Mol.Biol., 360:968-, 2006 Cited by PubMed Abstract: Cytochrome c6A is a unique dithio-cytochrome present in land plants and some green algae. Its sequence and occurrence in the thylakoid lumen suggest that it is derived from cytochrome c6, which functions in photosynthetic electron transfer between the cytochrome b6f complex and photosystem I. Its known properties, however, and a strong indication that the disulfide group is not purely structural, indicate that it has a different, unidentified function. To help in the elucidation of this function the crystal structure of cytochrome c6A from Arabidopsis thaliana has been determined in the two redox states of the heme group, at resolutions of 1.2 A (ferric) and 1.4 A (ferrous). These two structures were virtually identical, leading to the functionally important conclusion that the heme and disulfide groups do not communicate by conformational change. They also show, however, that electron transfer between the reduced disulfide and the heme is feasible. We therefore suggest that the role of cytochrome c6A is to use its disulfide group to oxidize dithiol/disulfide groups of other proteins of the thylakoid lumen, followed by internal electron transfer from the dithiol to the heme, and re-oxidation of the heme by another thylakoid oxidant. Consistent with this model, we found a rapid electron transfer between ferro-cytochrome c6A and plastocyanin, with a second-order rate constant, k2=1.2 x 10(7) M(-1) s(-1). PubMed: 16815443DOI: 10.1016/J.JMB.2006.05.065 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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