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Room temperature crystal structure of the fast switching M159T mutant of the fluorescent protein dronpa
Author(s) -
Kaucikas Marius,
Fitzpatrick Ann,
Bryan Elana,
Struve Abelone,
Henning Robert,
Kosheleva Irina,
Srajer Vukica,
Groenhof Gerrit,
Van Thor Jasper J.
Publication year - 2015
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24742
Subject(s) - fluorescence , fluorescent protein , mutant , green fluorescent protein , biophysics , temperature sensitive mutant , materials science , chemistry , crystallography , optics , biology , biochemistry , physics , gene
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‐Å resolution in the bright on state. Structural differences with the wild type include shifted backbone positions of strand β8 containing Thr159 as well as an altered A‐C dimer interface involving strands β7, β8, β10, and β11. 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. Proteins 2015; 83:397–402. © 2014 Wiley Periodicals, Inc.