Structural highlights
FunctionPublication Abstract from PubMedLight-Oxygen-Voltage (LOV) 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 that 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~11A movement of the C terminus in helix Jalpha, ~4A movement of Hbeta-Ibeta loop, disruption of hydrogen bonds in the dimer interface, and a~29 degrees 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'alpha-Abeta loop and the A'alpha 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. Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy.,Rollen K, Granzin J, Panwalkar V, Arinkin V, Rani R, Hartmann R, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R J Mol Biol. 2016 Jun 9. pii: S0022-2836(16)30206-6. doi:, 10.1016/j.jmb.2016.05.027. PMID:27291287[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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