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Structural photoactivation of a full-length bacterial phytochrome

Journal article
Authors Alexander Björling
Oskar Berntsson
H. Lehtivuori
Heikki Takala
Ashley J Hughes
Matthijs R Panman
Maria Hoernke
Stephan Niebling
Léocadie Henry
R. Henning
I. Kosheleva
V. Chukharev
N. V. Tkachenko
A. Menzel
G. Newby
D. Khakhulin
M. Wulff
J. A. Ihalainen
S. Westenhoff
Published in Science Advances
Volume 2
Issue 8
Pages artikel nr 1600920
ISSN 2375-2548
Publication year 2016
Published at Department of Chemistry and Molecular Biology
Pages artikel nr 1600920
Language en
Links dx.doi.org/10.1126/sciadv.1600920
Keywords x-ray-scattering, chromophore-binding domain, induced proton release, small-angle scattering, free-electron laser, histidine kinases, deinococcus-radiodurans, crystal-structure, flash-photolysis, ground-state, Science & Technology - Other Topics
Subject categories Biological Sciences

Abstract

Phytochromes are light sensor proteins found in plants, bacteria, and fungi. They function by converting a photon absorption event into a conformational signal that propagates from the chromophore through the entire protein. However, the structure of the photoactivated state and the conformational changes that lead to it are not known. We report time-resolved x-ray scattering of the full-length phytochrome from Deinococcus radiodurans on micro-and millisecond time scales. We identify a twist of the histidine kinase output domains with respect to the chromophore-binding domains as the dominant change between the photoactivated and resting states. The time-resolved data further show that the structural changes up to the microsecond time scales are small and localized in the chromophore-binding domains. The global structural change occurs within a few milliseconds, coinciding with the formation of the spectroscopic meta-Rc state. Our findings establish key elements of the signaling mechanism of full-length bacterial phytochromes.

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