Structural highlights
Function
CYCP_RUBGE Cytochrome c' is the most widely occurring bacterial c-type cytochrome. Cytochromes c' are high-spin proteins and the heme has no sixth ligand. Their exact function is not known.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
High resolution crystal structure of Rubrivivax gelatinosus cytochrome c'.,Benini S, Rypniewski WR, Wilson KS, Ciurli S J Inorg Biochem. 2008 May-Jun;102(5-6):1322-8. Epub 2008 Jan 21. PMID:18295896[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Benini S, Rypniewski WR, Wilson KS, Ciurli S. High resolution crystal structure of Rubrivivax gelatinosus cytochrome c'. J Inorg Biochem. 2008 May-Jun;102(5-6):1322-8. Epub 2008 Jan 21. PMID:18295896 doi:10.1016/j.jinorgbio.2008.01.017
