Structure of the photoactive yellow protein reconstituted with caffeic acid at 1.16 A resolution

Acta Crystallographica. Section D, Biological Crystallography
Daan M F van AaltenL Joshua-Tor

Abstract

A structural study is described of the photoactive yellow protein (PYP) reconstituted with the chromophore derivative 3,4-dihydroxycinnamic acid. The crystal structure of PYP reconstituted with this chromophore at 1.16 A resolution is reported in space group P6(5). This is the first high-resolution structure of a photoreceptor containing a modified chromophore. The introduction of an extra hydroxyl group in the native chromophore (i.e. p-coumaric acid) appears to perturb the structure of the hybrid yellow protein only slightly. The chromophore is bound by the protein in two different conformations, separated by a rotation of 180 degrees of the catechol ring. In combination with available spectroscopic data, it is concluded that the caffeic acid chromophore binds to the protein in a strained conformation, which leads to a faster ejection from the chromophore-binding pocket upon pB formation.

Citations

Apr 5, 2014·Chromosoma·Qiming Mei, Volodymyr Dvornyk
Jul 17, 2015·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Norio HamadaRyosuke Nakamura
May 10, 2007·Photochemical & Photobiological Sciences : Official Journal of the European Photochemistry Association and the European Society for Photobiology·Michael A van der HorstKlaas J Hellingwerf
Sep 14, 2019·Chembiochem : a European Journal of Chemical Biology·Jingchi GaoKazuya Kikuchi
Mar 18, 2003·The Journal of Biological Chemistry·Jocelyne VreedeDaan M F van Aalten
Aug 6, 2020·Journal of Photochemistry and Photobiology. A, Chemistry·Matthew G RomeiSteven G Boxer
Jul 10, 2003·Chemical Reviews·Christophe Dugave, Luc Demange

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