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| Hauptseite > Publikationsdatenbank > Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy |
| Hauptseite > Publikationsdatenbank > Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy |
| Journal Article | FZJ-2016-06320 |
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2016
Elsevier
Amsterdam [u.a.]
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Please use a persistent id in citations: doi:10.1016/j.jmb.2016.05.027
Abstract: Light–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 ~11 Å movement of the C terminus in helix Jα, ~4 Å movement of Hβ–Iβ 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′α–Aβ loop and the A′α 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.
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