Correlation Engine 2.0
Clear Search sequence regions

  • adduct (1)
  • apo (3)
  • flavin (2)
  • light (9)
  • oxygen (10)
  • protein binds (1)
  • pseudomonas putida (1)
  • vitro (1)
  • Sizes of these terms reflect their relevance to your search.

    Unique features of Light-Oxygen-Voltage (LOV) proteins like relatively small size (~12-19 kDa), inherent modularity, highly-tunable photocycle and oxygen-independent fluorescence have lately been exploited for the generation of optical tools. Structures of LOV domains reported so far contain a flavin chromophore per protein molecule. Here we report two new findings on the short LOV protein W619_1-LOV from Pseudomonas putida. First, the apo-state crystal structure of W619_1-LOV at 2.5 Å resolution reveals conformational rearrangements in the secondary structure elements lining the chromophore pocket including elongation of the Fα helix, shortening of the Eα-Fα loop and partial unfolding of the Eα helix. Second, the apo W619_1-LOV protein binds both natural and structurally modified flavin chromophores. Remarkably different photophysical and photochemical properties of W619_1-LOV bound to 7-methyl-8-chloro-riboflavin (8-Cl-RF) and lumichrome imply application of these variants as novel optical tools as they offer advantages such as no adduct state formation, and a broader choice of wavelengths for in vitro studies.


    Vladimir Arinkin, Joachim Granzin, Katrin Röllen, Ulrich Krauss, Karl-Erich Jaeger, Dieter Willbold, Renu Batra-Safferling. Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools. Scientific reports. 2017 Feb 17;7:42971

    PMID: 28211532

    View Full Text