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Issue 10, 2013
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A structural model for the full-length blue light-sensing protein YtvA from Bacillus subtilis, based on EPR spectroscopy

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Abstract

A model for the full-length structure of the blue light-sensing protein YtvA from Bacillus subtilis has been determined by EPR spectroscopy, performed on spin labels selectively inserted at amino acid positions 54, 80, 117 and 179. Our data indicate that YtvA forms a dimer in solution and enable us, based on the known structures of the individual domains and modelling, to propose a three-dimensional model for the full length protein. Most importantly, this includes the YtvA N-terminus that has so far not been identified in any structural model. We show that our data are in agreement with the crystal structure of an engineered LOV-domain protein, YF1, that shows the N-terminus of the protein to be helical and to fold back in between the β-sheets of the two LOV domains, and argue for an identical arrangement in YtvA. While we could not detect any structural changes upon blue-light activation of the protein, this structural model now forms an ideal basis for identifying residues as targets for further spin labelling studies to detect potential conformational changes upon irradiation of the protein.

Graphical abstract: A structural model for the full-length blue light-sensing protein YtvA from Bacillus subtilis, based on EPR spectroscopy

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Publication details

The article was received on 26 Apr 2013, accepted on 09 Jul 2013 and first published on 11 Jul 2013


Article type: Paper
DOI: 10.1039/C3PP50128K
Citation: Photochem. Photobiol. Sci., 2013,12, 1855-1863
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    A structural model for the full-length blue light-sensing protein YtvA from Bacillus subtilis, based on EPR spectroscopy

    C. Engelhard, S. Raffelberg, Y. Tang, R. P. Diensthuber, A. Möglich, A. Losi, W. Gärtner and R. Bittl, Photochem. Photobiol. Sci., 2013, 12, 1855
    DOI: 10.1039/C3PP50128K

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