Journal Article

FZJ-2018-04635

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein

Röllen, K.FZJ* ; Granzin, J.FZJ* ; Batra-Safferling, R. (Corresponding author)FZJ* ; Stadler, A. M. (Corresponding author)FZJ*

2018
PLoS Lawrence, Kan.

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Please use a persistent id in citations: http://hdl.handle.net/2128/19488  doi:10.1371/journal.pone.0200746

Abstract: 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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)
2. Neutronenstreuung (Neutronenstreuung ; JCNS-1)
3. Neutronenstreuung (ICS-1)

Research Program(s):

1. 551 - Functional Macromolecules and Complexes (POF3-551) (POF3-551)

Appears in the scientific report 2018

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Database coverage:
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