[NMR paper] Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy.

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Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy.

Related Articles Signaling states of a short blue light photoreceptor protein PpSB1-LOV revealed from crystal structures and solution NMR spectroscopy.

J Mol Biol. 2016 Jun 9;

Authors: Röllen K, Granzin J, Panwalkar V, Arinkin V, Rani R, Hartmann R, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R

Abstract
LOV (Light-Oxygen-Voltage) domains represent the photo-responsive domains of various blue-light photoreceptor proteins and are widely distributed in plants, algae, fungi and bacteria. Here, we report the dark state crystal structure of PpSB1-LOV, a slow-reverting short LOV protein from Pseudomonas putida which is remarkably different from our previously published 'fully light-adapted' structure [1]. A direct comparison of the two structures provides insight into the light-activated signaling mechanism. Major structural differences involve a~11Å movement of the C-terminus in helix J?, ~4Å movement of H?-I? loop, disruption of hydrogen bonds in the dimer interface, and a~29 ° rotation of chain-B relative to chain-A as compared to the light state dimer. Both, crystal structures and solution NMR data are suggestive of the key roles of a conserved glutamine Q116 and the N-cap region consisting of A'?-A? loop and the A'? helix in controlling the light-activated conformational changes. The activation mechanism proposed here for the PpSB1-LOV supports a rotary switch mechanism and provides insights into the signal propagation mechanism in naturally existing and artificial LOV-based two-component systems and regulators.


PMID: 27291287 [PubMed - as supplied by publisher]



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