5LUV

Short LOV protein W619_1 in apo-state

Summary for 5LUV

• Entry DOI: 10.2210/pdb5luv/pdb
• Descriptor: Putative PAS/PAC sensor protein, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: lov domain, pas domain, apo-state, signaling protein
• Biological source: Pseudomonas putida
• Total number of polymer chains: 2
• Total formula weight: 38589.90

Authors

Arinkin, V.,Granzin, J.,Batra-Safferling, R. (deposition date: 2016-09-12, release date: 2017-02-22, Last modification date: 2024-01-17)

Primary citation

Arinkin, V.,Granzin, J.,Rollen, K.,Krauss, U.,Jaeger, K.E.,Willbold, D.,Batra-Safferling, R.
Structure of a LOV protein in apo-state and implications for construction of LOV-based optical tools.
Sci Rep, 7:42971-42971, 2017

PubMed Abstract: 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.

PubMed: 28211532
DOI: 10.1038/srep42971

Experimental method

X-RAY DIFFRACTION (2.5 Å)