2J9B
THE CRYSTAL STRUCTURE OF CYTOCHROME C' FROM RUBRIVIVAX GELATINOSUS AT 1.5 A RESOLUTION AND PH 6.3
2J9B の概要
| エントリーDOI | 10.2210/pdb2j9b/pdb |
| 関連するPDBエントリー | 1JAF 2J8W |
| 分子名称 | CYTOCHROME C', HEME C (3 entities in total) |
| 機能のキーワード | heme, iron, transport, metal-binding, electron transfer, electron transport |
| 由来する生物種 | RHODOCYCLUS GELATINOSUS |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 27843.12 |
| 構造登録者 | Benini, S.,Ciurli, S.,Rypniewski, W.R.,Wilson, K.S. (登録日: 2006-11-06, 公開日: 2007-12-04, 最終更新日: 2024-10-09) |
| 主引用文献 | Benini, S.,Rypniewski, W.R.,Wilson, K.S.,Ciurli, S. High resolution crystal structure of Rubrivivax gelatinosus cytochrome c'. J. Inorg. Biochem., 102:1322-1328, 2008 Cited by PubMed Abstract: The structure of the cytochrome c' from the purple non-sulfur phototrophic bacterium Rubrivivax gelatinosus was determined using two crystals grown independently at pH 6.3 and pH 8. The resolution attained for the two structures (1.29 A and 1.50 A for the crystals at high and low pH, respectively) is the highest to date for this class of proteins. The two structures were compared in detail in an attempt to investigate the influence of pH on the geometry of the haem and of the coordination environment of the Fe(III) ion. However, while the results suggest some small propensity for the movement of the metal atom out of the plane of the haem ring upon pH increase, the accuracy of the measurements at these two pH below the pK of the axial histidine is not sufficient to provide hard evidence of a shift in the iron position and associated changes. PubMed: 18295896DOI: 10.1016/j.jinorgbio.2008.01.017 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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