Room temperature crystal structure of the fast switching M159T mutant of the fluorescent protein dronpa |
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| Authors: | Marius Kaucikas Ann Fitzpatrick Elana Bryan Abelone Struve Robert Henning Irina Kosheleva Vukica Srajer Gerrit Groenhof Jasper J. Van Thor |
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| Affiliation: | 1. Division of Molecular Biosciences, Imperial College London, London, United Kingdom;2. Department of Chemistry, University of Chicago, Chicago, Illinois;3. Department of Biochemistry and Molecular Biology, Center for Advanced Radiation Sources (CARS), University of Chicago, Chicago, Illinois;4. Department of Chemistry and Nanoscience Center, University of Jyv?skyl?, Jyv?skyl?, Finland |
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| Abstract: | 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. |
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| Keywords: | Dronpa reversibly photoswitchable fluorescent protein X‐ray structure room temperature molecular dynamics |
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