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Structural basis for the influence of a single mutation K145N on the oligomerization and photoswitching rate of Dronpa

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Abstract
The crystal structure of the on-state of PDM1-4, a single-mutation variant of the photochromic fluorescent protein Dronpa, is reported at 1.95 angstrom resolution. PDM1-4 is a Dronpa variant that possesses a slower off-switching rate than Dronpa and thus can effectively increase the image resolution in subdiffraction optical microscopy, although the precise molecular basis for this change has not been elucidated. This work shows that the Lys145Asn mutation in PDM1-4 stabilizes the interface available for dimerization, facilitating oligomerization of the protein. No significant changes were observed in the chromophore environment of PDM1-4 compared with Dronpa, and the ensemble absorption and emission properties of PDM1-4 were highly similar to those of Dronpa. It is proposed that the slower off-switching rate in PDM1-4 is caused by a decrease in the potential flexibility of certain beta-strands caused by oligomerization along the AC interface.
Keywords
FLUORESCENT PROTEIN DRONPA, GENERATION, RED FLUORESCENCE

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Chicago
Nguyen Bich, Ngan, Benjamien Moeyaert, Kristof Van Hecke, Peter Dedecker, Hideaki Mizuno, Johan Hofkens, and Luc Van Meervelt. 2012. “Structural Basis for the Influence of a Single Mutation K145N on the Oligomerization and Photoswitching Rate of Dronpa.” Acta Crystallographica Section D-biological Crystallography 68 (12): 1653–1659.
APA
Nguyen Bich, N., Moeyaert, B., Van Hecke, K., Dedecker, P., Mizuno, H., Hofkens, J., & Van Meervelt, L. (2012). Structural basis for the influence of a single mutation K145N on the oligomerization and photoswitching rate of Dronpa. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 68(12), 1653–1659.
Vancouver
1.
Nguyen Bich N, Moeyaert B, Van Hecke K, Dedecker P, Mizuno H, Hofkens J, et al. Structural basis for the influence of a single mutation K145N on the oligomerization and photoswitching rate of Dronpa. ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. 2012;68(12):1653–9.
MLA
Nguyen Bich, Ngan, Benjamien Moeyaert, Kristof Van Hecke, et al. “Structural Basis for the Influence of a Single Mutation K145N on the Oligomerization and Photoswitching Rate of Dronpa.” ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY 68.12 (2012): 1653–1659. Print.
@article{3103435,
  abstract     = {The crystal structure of the on-state of PDM1-4, a single-mutation variant of the photochromic fluorescent protein Dronpa, is reported at 1.95 angstrom resolution. PDM1-4 is a Dronpa variant that possesses a slower off-switching rate than Dronpa and thus can effectively increase the image resolution in subdiffraction optical microscopy, although the precise molecular basis for this change has not been elucidated. This work shows that the Lys145Asn mutation in PDM1-4 stabilizes the interface available for dimerization, facilitating oligomerization of the protein. No significant changes were observed in the chromophore environment of PDM1-4 compared with Dronpa, and the ensemble absorption and emission properties of PDM1-4 were highly similar to those of Dronpa. It is proposed that the slower off-switching rate in PDM1-4 is caused by a decrease in the potential flexibility of certain beta-strands caused by oligomerization along the AC interface.},
  author       = {Nguyen Bich, Ngan and Moeyaert, Benjamien and Van Hecke, Kristof and Dedecker, Peter and Mizuno, Hideaki and Hofkens, Johan and Van Meervelt, Luc},
  issn         = {0907-4449},
  journal      = {ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY},
  keyword      = {FLUORESCENT PROTEIN DRONPA,GENERATION,RED FLUORESCENCE},
  language     = {eng},
  number       = {12},
  pages        = {1653--1659},
  title        = {Structural basis for the influence of a single mutation K145N on the oligomerization and photoswitching rate of Dronpa},
  url          = {http://dx.doi.org/10.1107/S0907444912039686},
  volume       = {68},
  year         = {2012},
}

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