This title appears in the Scientific Report :
2016
Please use the identifier:
http://dx.doi.org/10.1016/j.jmb.2016.05.027 in citations.
Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy
Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy
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...
| Personal Name(s): | Röllen, Katrin |
|---|---|
| Granzin, Joachim / Panwalkar, Vineet / Arinkin, Vladimir / Rani, Raj / Hartmann, Rudolf / Krauss, Ulrich / Jaeger, Karl-Erich / Willbold, Dieter / Batra-Safferling, Renu (Corresponding author) | |
| Contributing Institute: |
Institut für Molekulare Enzymtechnologie (HHUD); IMET Strukturbiochemie; ICS-6 |
| Published in: | Journal of molecular biology, 428 (2016) 19, S. 3721 - 3736 |
| Imprint: |
Amsterdam [u.a.]
Elsevier
2016
|
| PubMed ID: |
27291287 |
| DOI: |
10.1016/j.jmb.2016.05.027 |
| Document Type: |
Journal Article |
| Research Program: |
Biotechnology Physical Basis of Diseases |
| Publikationsportal JuSER |
|
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. |