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Common Structural Elements in the Chromophore Binding Pocket of the Pfr State of Bathy Phytochromes
Citation key ISI:000401262000011
Author Escobar, Francisco Velazquez and Buhrke, David and Michael, Norbert and Sauthof, Luisa and Wilkening, Svea and Tavraz, Neslihan N. and Salewski, Johannes and Frankenberg-Dinkel, Nicole and Mroginski, Maria Andrea and Scheerer, Patrick and Friedrich, Thomas and Siebert, Friedrich and Hildebrandt, Peter
Pages 724-732
Year 2017
ISSN 0031-8655
DOI 10.1111/php.12742
Address 111 RIVER ST, HOBOKEN 07030-5774, NJ USA
Volume 93
Number 3
Publisher WILEY
Abstract Phytochromes are bimodal photoreceptors which, upon light absorption by the tetrapyrrole chromophore, can be converted between a red-absorbing state (Pr) and far-red-absorbing state (Pfr). In bacterial phytochromes, either Pr or Pfr are the thermally stable states, thereby constituting the classes of prototypical and bathy phytochromes, respectively. In this work, we have employed vibrational spectroscopies to elucidate the origin of the thermal stability of the Pfr states in bathy phytochromes. Here, we present the first detailed spectroscopic analysis of RpBphP6 (Rhodopseudomas palustris), which together with results obtained for Agp2 (Agrobacterium tumefaciens) and PaBphP (Pseudomonas aeruginosa) allows identifying common structural properties of the Pfr state of bathy phytochromes, which are (1) a homogenous chromophore structure, (2) the protonated ring C propionic side chain of the chromophore and (3) a retarded H/D exchange at the ring D nitrogen. These properties are related to the unique strength of the hydrogen bonding interactions between the ring D N-H group with the side chain of the conserved Asp194 (PaBphP numbering). As revealed by a comparative analysis of homology models and available crystal structures of Pfr states, these interactions are strengthened by an Arg residue (Arg453) only in bathy but not in prototypical phytochromes.
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