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4EMQ

Crystal structure of a single mutant of Dronpa, the green-on-state PDM1-4

Summary for 4EMQ
Entry DOI10.2210/pdb4emq/pdb
Related2z1o 2z6y 2z6z
DescriptorFluorescent protein Dronpa, 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID, PENTAETHYLENE GLYCOL, ... (5 entities in total)
Functional Keywordsdronpa, gfp-like protein, reversible photoswitchable fluorescent protein, beta barrel, fluorescent protein
Biological sourceEchinophyllia sp. SC22
Total number of polymer chains6
Total formula weight177802.26
Authors
Ngan, N.B.,Van Hecke, K.,Van Meervelt, L. (deposition date: 2012-04-12, release date: 2012-11-21, Last modification date: 2024-10-09)
Primary citationNguyen Bich, N.,Moeyaert, B.,Van Hecke, K.,Dedecker, P.,Mizuno, H.,Hofkens, J.,Van Meervelt, L.
Structural basis for the influence of a single mutation K145N on the oligomerization and photoswitching rate of Dronpa.
Acta Crystallogr.,Sect.D, 68:1653-1659, 2012
Cited by
PubMed 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 Å 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 β-strands caused by oligomerization along the AC interface.
PubMed: 23151630
DOI: 10.1107/S0907444912039686
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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数据于2024-11-06公开中

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