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2J9B

THE CRYSTAL STRUCTURE OF CYTOCHROME C' FROM RUBRIVIVAX GELATINOSUS AT 1.5 A RESOLUTION AND PH 6.3

Summary for 2J9B
Entry DOI10.2210/pdb2j9b/pdb
Related1JAF 2J8W
DescriptorCYTOCHROME C', HEME C (3 entities in total)
Functional Keywordsheme, iron, transport, metal-binding, electron transfer, electron transport
Biological sourceRHODOCYCLUS GELATINOSUS
Total number of polymer chains2
Total formula weight27843.12
Authors
Benini, S.,Ciurli, S.,Rypniewski, W.R.,Wilson, K.S. (deposition date: 2006-11-06, release date: 2007-12-04, Last modification date: 2024-10-09)
Primary citationBenini, 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: 18295896
DOI: 10.1016/j.jinorgbio.2008.01.017
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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数据于2025-07-23公开中

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