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* Department of Biochemistry and Molecular Biology,
Edited by Vincent Massey, University of Michigan Medical School,
Ann Arbor, MI, and approved January 3, 2001 (received for review October 31, 2000)
Phototropin, a major blue-light receptor for phototropism in seed
plants, exhibits blue-light-dependent autophosphorylation and contains
two light, oxygen, or voltage (LOV) domains and a serine/threonine
kinase domain. The LOV domains share homology with the PER-ARNT-SIM
(PAS) superfamily, a diverse group of sensor proteins. Each LOV domain
noncovalently binds a single FMN molecule and exhibits reversible
photochemistry in vitro when expressed separately or in
tandem. We have determined the crystal structure of the LOV2 domain
from the phototropin segment of the chimeric fern photoreceptor phy3 to
2.7-Å resolution. The structure constitutes an FMN-binding fold that
reveals how the flavin cofactor is embedded in the protein. The
single LOV2 cysteine residue is located 4.2 Å from flavin atom C(4a),
consistent with a model in which absorption of blue light induces
formation of a covalent cysteinyl-C(4a) adduct. Residues that interact
with FMN in the phototropin segment of the chimeric fern photoreceptor
(phy3) LOV2 are conserved in LOV domains from phototropin of other
plant species and from three proteins involved in the regulation of
circadian rhythms in Arabidopsis and
Neurospora. This conservation suggests that these
domains exhibit the same overall fold and share a common mechanism
for flavin binding and light-induced signaling.
Biochemistry
Structure of a flavin-binding plant photoreceptor domain:
Insights into light-mediated signal transduction
and
,
,§
Center for Advanced Radiation Sources, and
§ Institute for Biophysical Dynamics, University of
Chicago, 920 East 58th Street, Chicago, IL 60637
To whom reprint requests should be addressed. E-mail:
scrosson{at}midway.uchicago.edu or moffat{at}cars.uchicago.edu.
www.pnas.org/cgi/doi/10.1073/pnas.051520298
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