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1jnu

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(New page: 200px<br /><applet load="1jnu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jnu, resolution 2.60&Aring;" /> '''Photoexcited structu...)
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Revision as of 21:48, 24 November 2007

Image:1jnu.gif

1jnu, resolution 2.60Å

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Photoexcited structure of the plant photoreceptor domain, phy3 LOV2

Overview

The phototropins are flavoprotein kinases that control phototropic, bending, light-induced chloroplast movement, and stomatal opening in, plants. Two flavin mononucleotide binding light, oxygen, or voltage (LOV), domains are the sites for initial photochemistry in these blue light, photoreceptors. We have determined the steady state, photoexcited crystal, structure of a flavin-bound LOV domain. The structure reveals a unique, photochemical switch in the flavin binding pocket in which the absorption, of light drives the formation of a reversible covalent bond between a, highly conserved Cys residue and the flavin cofactor. This provides a, molecular picture of a cysteinyl-flavin covalent adduct, the presumed, signaling species that leads to phototropin kinase activation and, subsequent signal transduction. We identify closely related LOV domains in, two eubacterial proteins that suggests the light-induced conformational, change evident in this structure is an ancient biomolecular response to, light, arising before the appearance of plants.

About this Structure

1JNU is a Single protein structure of sequence from Eukaryota with FMN as ligand. Full crystallographic information is available from OCA.

Reference

Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch., Crosson S, Moffat K, Plant Cell. 2002 May;14(5):1067-75. PMID:12034897

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