2pr6: Difference between revisions

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[[Image:2pr6.jpg|left|200px]]
[[Image:2pr6.jpg|left|200px]]


{{Structure
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|PDB= 2pr6 |SIZE=350|CAPTION= <scene name='initialview01'>2pr6</scene>, resolution 1.950&Aring;
The line below this paragraph, containing "STRUCTURE_2pr6", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>
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|GENE= pfyP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])
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|DOMAIN=
{{STRUCTURE_2pr6| PDB=2pr6  | SCENE= }}  
|RELATEDENTRY=[[2pr5|2PR5]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2pr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pr6 OCA], [http://www.ebi.ac.uk/pdbsum/2pr6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2pr6 RCSB]</span>
}}


'''Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Light Structure)'''
'''Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Light Structure)'''
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[[Category: Moffat, K.]]
[[Category: Moffat, K.]]
[[Category: Moglich, A.]]
[[Category: Moglich, A.]]
[[Category: flavoprotein]]
[[Category: Flavoprotein]]
[[Category: light-oxygen-voltage]]
[[Category: Light-oxygen-voltage]]
[[Category: lov]]
[[Category: Lov]]
[[Category: pa]]
[[Category: Pa]]
[[Category: per-arnt-sim]]
[[Category: Per-arnt-sim]]
[[Category: signaling protein]]
[[Category: Signaling protein]]
 
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Revision as of 13:40, 4 May 2008

File:2pr6.jpg

Template:STRUCTURE 2pr6

Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Light Structure)


OverviewOverview

The photosensor YtvA binds flavin mononucleotide and regulates the general stress reaction in Bacillus subtilis in response to blue light illumination. It belongs to the family of light-oxygen-voltage (LOV) proteins that were first described in plant phototropins and form a subgroup of the Per-Arnt-Sim (PAS) superfamily. Here, we report the three-dimensional structure of the LOV domain of YtvA in its dark and light states. The protein assumes the global fold common to all PAS domains and dimerizes via a hydrophobic interface. Directly C-terminal to the core of the LOV domain, an alpha-helix extends into the solvent. Light absorption causes formation of a covalent bond between a conserved cysteine residue and atom C(4a) of the FMN ring, which triggers rearrangements throughout the LOV domain. Concomitantly, in the dark and light structures, the two subunits of the dimeric protein rotate relative to each other by 5 degrees . This small quaternary structural change is presumably a component of the mechanism by which the activity of YtvA is regulated in response to light. In terms of both structure and signaling mechanism, YtvA differs from plant phototropins and more closely resembles prokaryotic heme-binding PAS domains.

About this StructureAbout this Structure

2PR6 is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA., Moglich A, Moffat K, J Mol Biol. 2007 Oct 12;373(1):112-26. Epub 2007 Aug 2. PMID:17764689 Page seeded by OCA on Sun May 4 13:40:12 2008

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