Structural highlights
Function
[BPHY_DEIRA] Photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region. Has also a slight blue shift for the far-red maximum. Could also absorb green light. May participate in regulating pigment synthesis like the carotenoid deinoxanthin which could protect the bacterium from intense visible light.
Publication Abstract from PubMed
We report that in the red light-absorbing (Pr) state, the bilin chromophore of the Deinococcus radiodurans proteobacterial phytochrome (DrBphP) is hypersensitive to X-ray photons used in typical synchrotron X-ray protein crystallography experiments. This causes the otherwise fully protonated chromophore to deprotonate without additional major structural changes. These results have major implications for our understanding of the structural and chemical characteristics of the resting and intermediate states of phytochromes and other photoreceptor proteins.
X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome.,Li F, Burgie ES, Yu T, Heroux A, Schatz GC, Vierstra RD, Orville AM J Am Chem Soc. 2015 Mar 4;137(8):2792-5. doi: 10.1021/ja510923m. Epub 2015 Feb, 18. PMID:25650486[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li F, Burgie ES, Yu T, Heroux A, Schatz GC, Vierstra RD, Orville AM. X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome. J Am Chem Soc. 2015 Mar 4;137(8):2792-5. doi: 10.1021/ja510923m. Epub 2015 Feb, 18. PMID:25650486 doi:http://dx.doi.org/10.1021/ja510923m
