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Publication Abstract from PubMed

The fluorescent protein Dronpa undergoes reversible photoswitching reactions between the bright "on" and dark "off" states via photoisomerization and proton transfer reactions. We report the room temperature crystal structure of the fast switching Met159Thr mutant of Dronpa at 2.0-A resolution in the bright on state. Structural differences with the wild type include shifted backbone positions of strand beta8 containing Thr159 as well as an altered A-C dimer interface involving strands beta7, beta8, beta10, and beta11. The Met159Thr mutation increases the cavity volume for the p-hydroxybenzylidene-imidazolinone chromophore as a result of both the side chain difference and the backbone positional differences.

Room temperature crystal structure of the fast switching M159T mutant of the fluorescent protein dronpa.,Kaucikas M, Fitzpatrick A, Bryan E, Struve A, Henning R, Kosheleva I, Srajer V, Groenhof G, Van Thor JJ Proteins. 2015 Mar;83(3):397-402. doi: 10.1002/prot.24742. Epub 2015 Jan 13. PMID:25524427^[1]

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