2PR5
Structural Basis for Light-dependent Signaling in the Dimeric LOV Photosensor YtvA (Dark Structure)
Summary for 2PR5
| Entry DOI | 10.2210/pdb2pr5/pdb |
| Related | 2PR6 |
| Descriptor | Blue-light photoreceptor, SODIUM ION, FLAVIN MONONUCLEOTIDE, ... (5 entities in total) |
| Functional Keywords | light-oxygen-voltage, lov, per-arnt-sim, pas, flavoprotein, signaling protein |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 2 |
| Total formula weight | 31295.67 |
| Authors | Moglich, A.,Moffat, K. (deposition date: 2007-05-03, release date: 2007-08-07, Last modification date: 2024-02-21) |
| Primary citation | Moglich, A.,Moffat, K. Structural Basis for Light-dependent Signaling in the Dimeric LOV Domain of the Photosensor YtvA. J.Mol.Biol., 373:112-126, 2007 Cited by PubMed Abstract: 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. PubMed: 17764689DOI: 10.1016/j.jmb.2007.07.039 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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