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

Ngan Nguyen Bich, Benjamien Moeyaert, Kristof Van Hecke UGent, Peter Dedecker, Hideaki Mizuno, Johan Hofkens and Luc Van Meervelt (2012) ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. 68(12). p.1653-1659
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.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
FLUORESCENT PROTEIN DRONPA, GENERATION, RED FLUORESCENCE
journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
Acta Crystallogr. Sect. D-Biol. Crystallogr.
volume
68
issue
12
pages
1653 - 1659
Web of Science type
Article
Web of Science id
000311097200007
JCR category
BIOPHYSICS
JCR impact factor
14.103 (2012)
JCR rank
1/71 (2012)
JCR quartile
1 (2012)
ISSN
0907-4449
DOI
10.1107/S0907444912039686
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
3103435
handle
http://hdl.handle.net/1854/LU-3103435
date created
2013-01-22 10:44:57
date last changed
2018-01-29 12:13:00
@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},
}

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.