Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion.

@article{Yang2007CrystalSO,
  title={Crystal structure of the chromophore binding domain of an unusual bacteriophytochrome, RpBphP3, reveals residues that modulate photoconversion.},
  author={Xiaojing Yang and Emina A. Stojkovi{\'c} and Jane Kuk and Keith Moffat},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2007},
  volume={104 30},
  pages={12571-6}
}
Bacteriophytochromes RpBphP2 and RpBphP3 from the photosynthetic bacterium Rhodopseudomonas palustris work in tandem to modulate synthesis of the light-harvesting complex LH4 in response to light. Although RpBphP2 and RpBphP3 share the same domain structure with 52% sequence identity, they demonstrate distinct photoconversion behaviors. RpBphP2 exhibits the "classical" phytochrome behavior of reversible photoconversion between red (Pr) and far-red (Pfr) light-absorbing states, whereas RpBphP3… CONTINUE READING

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