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Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA

Title data

Möglich, Andreas ; Moffat, Keith:
Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA.
In: Journal of Molecular Biology. Vol. 373 (12 October 2007) Issue 1 . - pp. 112-126.
ISSN 0022-2836
DOI: https://doi.org/10.1016/j.jmb.2007.07.039

Project information

Project financing: National Institutes of Health

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 10924135
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 20 May 2015 06:48
Last Modified: 20 May 2015 06:48
URI: https://eref.uni-bayreuth.de/id/eprint/13610