2J8W
The crystal structure of cytochrome c' from Rubrivivax gelatinosus at 1.3 A Resolution and pH 8.0
Summary for 2J8W
| Entry DOI | 10.2210/pdb2j8w/pdb |
| Related | 1JAF |
| Descriptor | CYTOCHROME C', HEME C (3 entities in total) |
| Functional Keywords | c', heme, iron, transport, cytochrome, metal-binding, electron transfer, electron transport, rubrivivax gelatinosus |
| Biological source | RUBRIVIVAX GELATINOSUS |
| Total number of polymer chains | 2 |
| Total formula weight | 27843.12 |
| Authors | Benini, S.,Ciurli, S.,Rypniewski, W.R.,Wilson, K.S. (deposition date: 2006-10-30, release date: 2007-11-06, Last modification date: 2024-10-23) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.29 Å) |
Structure validation
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