Open AccessFTIR Spectroscopy Revealing Light-Dependent Refolding of the Conserved Tongue Region of Bacteriophytochrome
Author(s) -
Emina A. Stojković,
K.C. Toh,
Maxime Alexandre,
Marian Baclayon,
Keith Moffat,
John T. M. Kennis
Publication year - 2014
Publication title -
the journal of physical chemistry letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.563
H-Index - 203
ISSN - 1948-7185
DOI - 10.1021/jz501189t
Subject(s) - deinococcus radiodurans , phy , fourier transform infrared spectroscopy , spectroscopy , chemistry , helix (gastropod) , tongue , crystallography , biophysics , protein secondary structure , photochemistry , biology , biochemistry , physics , optics , dna , medicine , computer science , physical layer , telecommunications , ecology , pathology , quantum mechanics , snail , wireless
Bacteriophytochromes (BphPs) constitute a class of photosensory proteins that toggle between Pr and Pfr functional states through absorption of red and far-red light. The photosensory core of BphPs is composed of PAS, GAF, and PHY domains. Here, we apply FTIR spectroscopy to investigate changes in the secondary structure of Rhodopseudomonas palustris BphP2 (RpBphP2) upon Pr to Pfr photoconversion. Our results indicate conversion from a β-sheet to an α-helical element in the so-called tongue region of the PHY domain, consistent with recent X-ray structures of Deinococcus radiodurans DrBphP in dark and light states (Takala H.; et al. Nature2014, 5, 245-248). A conserved Asp in the GAF domain that noncovalently connects with the PHY domain and a conserved Pro in the tongue region of the PHY domain are essential for the β-sheet-to-α-helix conversion.
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