5luv

Publication Abstract from PubMed

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 A resolution reveals conformational rearrangements in the secondary structure elements lining the chromophore pocket including elongation of the Falpha helix, shortening of the Ealpha-Falpha loop and partial unfolding of the Ealpha 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.

Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools.,Arinkin V, Granzin J, Rollen K, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R Sci Rep. 2017 Feb 17;7:42971. doi: 10.1038/srep42971. PMID:28211532^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.