This title appears in the Scientific Report :
2018
Please use the identifier:
http://hdl.handle.net/2128/19488 in citations.
Please use the identifier: http://dx.doi.org/10.1371/journal.pone.0200746 in citations.
Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein
Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein
Light, oxygen, voltage (LOV) photoreceptors consist of conserved photo-responsive domains in bacteria, archaea, plants and fungi, and detect blue-light via a flavin cofactor. We investigated the blue-light induced conformational transition of the dimeric photoreceptor PpSB1-LOV-R66I from Pseudomonas...
Saved in:
Personal Name(s): | Röllen, Katrin |
---|---|
Granzin, Joachim / Batra-Safferling, Renu (Corresponding author) / Stadler, Andreas Maximilian (Corresponding author) | |
Contributing Institute: |
Neutronenstreuung; ICS-1 Neutronenstreuung; JCNS-1 Strukturbiochemie; ICS-6 |
Published in: | PLoS one, 13 (2018) 7, S. e0200746 |
Imprint: |
Lawrence, Kan.
PLoS
2018
|
DOI: |
10.1371/journal.pone.0200746 |
PubMed ID: |
30011332 |
Document Type: |
Journal Article |
Research Program: |
Functional Macromolecules and Complexes |
Link: |
OpenAccess OpenAccess |
Publikationsportal JuSER |
Please use the identifier: http://dx.doi.org/10.1371/journal.pone.0200746 in citations.
Light, oxygen, voltage (LOV) photoreceptors consist of conserved photo-responsive domains in bacteria, archaea, plants and fungi, and detect blue-light via a flavin cofactor. We investigated the blue-light induced conformational transition of the dimeric photoreceptor PpSB1-LOV-R66I from Pseudomonas putida in solution by using small-angle X-ray scattering (SAXS). SAXS experiments of the fully populated light- and dark-states under steady-state conditions revealed significant structural differences between the two states that are in agreement with the known structures determined by crystallography. We followed the transition from the light- to the dark-state by using SAXS measurements in real-time. A two-state model based on the light- and dark-state conformations could describe the measured time-course SAXS data with a relaxation time τREC of ~ 34 to 35 min being larger than the recovery time found with UV/vis spectroscopy. Unlike the flavin chromophore-based UV/vis method that is sensitive to the local chromophore environment in flavoproteins, SAXS-based assay depends on protein conformational changes and provides with an alternative to measure the recovery kinetics. |