Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 291, Issue 28, Pages 14839-14850Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M116.731448
Keywords
kinetics; molecular dynamics; optogenetics; photobiology; structure-function; LOV domain; osmotic stress
Categories
Funding
- Herman Frasch Foundation [739-HF12]
- Austrian Science Fund Project [P24350-B20]
- Austrian Science Fund (FWF) [P 24350] Funding Source: researchfish
- Austrian Science Fund (FWF) [P24350] Funding Source: Austrian Science Fund (FWF)
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Light-oxygen-voltage (LOV) domain-containing proteins function as small light-activated modules capable of imparting blue light control of biological processes. Their small modular nature has made them model proteins for allosteric signal transduction and optogenetic devices. Despite intense research, key aspects of their signal transduction mechanisms and photochemistry remain poorly understood. In particular, ordered water has been identified as a possible key mediator of photocycle kinetics, despite the lack of ordered water in the LOV active site. Herein, we use recent crystal structures of a fungal LOV protein ENVOY to interrogate the role of Thr(101) in recruiting water to the flavin active site where it can function as an intrinsic base to accelerate photocycle kinetics. Kinetic and molecular dynamic simulations confirm a role in solvent recruitment to the active site and identify structural changes that correlate with solvent recruitment. In vivo analysis of T101I indicates a direct role of the Thr(101) position in mediating adaptation to osmotic stress, thereby verifying biological relevance of ordered water in LOV signaling. The combined studies identify position 101 as a mediator of both allostery and photocycle catalysis that can impact organism physiology.
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