2pr5
From Proteopedia
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Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Dark Structure)
Overview
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 Structure
2PR5 is a Single protein structure of sequence from Bacillus subtilis with NA, FMN and ACY as ligands. Full crystallographic information is available from OCA.
Reference
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 Wed Nov 21 13:37:35 2007
Categories: Bacillus subtilis | Single protein | Moffat, K. | Moglich, A. | ACY | FMN | NA | Flavoprotein | Light-oxygen-voltage | Lov | Pas | Per-arnt-sim | Signaling protein
