Abstract:
: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-A 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 A 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.
journal_name
Proc Natl Acad Sci U S Aauthors
Crosson S,Moffat Kdoi
10.1073/pnas.051520298keywords:
subject
Has Abstractpub_date
2001-03-13 00:00:00pages
2995-3000issue
6eissn
0027-8424issn
1091-6490pii
051520298journal_volume
98pub_type
杂志文章abstract::Two deletion-substitution mutations of phage lambda, spi-113 and spi-274, are shown to remove about half of the rightward operator OR. Physiological studies show that spi-113 is still repressible. Thus, the 50 or so nucleotides of OR deleted in this mutant are not absolutely essential for repression. prm-116, which in...
journal_title:Proceedings of the National Academy of Sciences of the United States of America
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journal_title:Proceedings of the National Academy of Sciences of the United States of America
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