1jnu: Difference between revisions

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New page: left|200px<br /><applet load="1jnu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jnu, resolution 2.60Å" /> '''Photoexcited structu...
 
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[[Image:1jnu.gif|left|200px]]<br /><applet load="1jnu" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jnu.gif|left|200px]]<br /><applet load="1jnu" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jnu, resolution 2.60&Aring;" />
caption="1jnu, resolution 2.60&Aring;" />
'''Photoexcited structure of the plant photoreceptor domain, phy3 LOV2'''<br />
'''Photoexcited structure of the plant photoreceptor domain, phy3 LOV2'''<br />


==Overview==
==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.
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==
==About this Structure==
1JNU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JNU OCA].  
1JNU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eukaryota Eukaryota] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JNU OCA].  


==Reference==
==Reference==
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[[Category: plant photoreceptor]]
[[Category: plant photoreceptor]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sat Nov 24 23:55:40 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:24:50 2008''

Revision as of 14:24, 21 February 2008

File:1jnu.gif


1jnu, resolution 2.60Å

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Photoexcited structure of the plant photoreceptor domain, phy3 LOV2

OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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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