Structural highlights
Publication Abstract from PubMedLight, 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 tauREC 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. Small-angle X-ray scattering study of the kinetics of light-dark transition in a LOV protein.,Rollen K, Granzin J, Batra-Safferling R, Stadler AM PLoS One. 2018 Jul 16;13(7):e0200746. doi: 10.1371/journal.pone.0200746., eCollection 2018. PMID:30011332[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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