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Comparison List

PDM1-4

PDM1-4 is a fluorescent protein published in 2010, derived from Echinophyllia sp. SC22. It is reported to be a tetramer.

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Oligomerization Organism Molecular Weight Cofactor
Tetramer Echinophyllia sp. SC22 25.5 kDa -

FPbase ID: XTCUL

Attributes

This protein does not yet have any fluorescent states assigned. Submit a change.

Photostability

No photostability measurements available ... add one!

PDM1-4 Sequence

BLAST

PDM1-4 was derived from Dronpa with the following mutations: K145N

MSVIKPDMKIKLRMEGAVNGHPFAIEGVGLGKPFEGKQSMDLKVKEGGPLPFAYDILTTVFCYGNRVFAKYPENIVDYFKQSFPEGYSWERSMNYEDGGICNATNDITLDGDCYIYEIRFDGVNFPANGPVMQKRTVKWEPSTENLYVRDGVLKGDVNMALSLEGGGHYRCDFKTTYKAKKVVQLPDYHFVDHHIEIKSHDKDYSNVNLHEHAEAHSELPRQAK

Structure

Deposited: ,
Chromophore:

Excerpts

An attempt to find Dronpa variants with slower off-switching rate has led to the identification of PDM1-4. Unfortunately, PDM1-4 was prone to form tetramers and did not show improvement in photon output. In addition, PDM1-4 has worsened photostability and less contrast between on and off-states.

Chang et al. (2012)

Primary Reference

Higher resolution in localization microscopy by slower switching of a photochromic protein

Mizuno H, Dedecker P, Ando R, Fukano T, Hofkens J, Miyawaki A

(2010). Photochemical & Photobiological Sciences, 9(2) , 239. doi: 10.1039/b9pp00124g. Article   Pubmed

Additional References

  1. A unique series of reversibly switchable fluorescent proteins with beneficial properties for various applications

    Chang H, Zhang M, Ji W, Chen J, Zhang Y, Liu B, Lu J, Zhang J, Xu P, Xu T

    (2012). Proceedings of the National Academy of Sciences, 109(12) , 4455-4460. doi: 10.1073/pnas.1113770109. Article   Pubmed

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

    Nguyen Bich N, Moeyaert B, Van Hecke K, Dedecker P, Mizuno H, Hofkens J, Van Meervelt L

    (2012). Acta Crystallographica Section D Biological Crystallography, 68(12) , 1653-1659. doi: 10.1107/s0907444912039686. Article   Pubmed

External Resources

Change history

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