TY  - JOUR
AU  - Röllen, Katrin
AU  - Granzin, Joachim
AU  - Panwalkar, Vineet
AU  - Arinkin, Vladimir
AU  - Rani, Raj
AU  - Hartmann, Rudolf
AU  - Krauss, Ulrich
AU  - Jaeger, Karl-Erich
AU  - Willbold, Dieter
AU  - Batra-Safferling, Renu
TI  - Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy
JO  - Journal of molecular biology
VL  - 428
IS  - 19
SN  - 0022-2836
CY  - Amsterdam [u.a.]
PB  - Elsevier
M1  - FZJ-2016-06320
SP  - 3721 - 3736
PY  - 2016
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000384383400005
C6  - pmid:27291287
DO  - DOI:10.1016/j.jmb.2016.05.027
UR  - https://juser.fz-juelich.de/record/821076
ER  -