ArticleJournal of microbiology (Seoul, Korea)2018
Spectral and structural analysis of large Stokes shift fluorescent protein dKeima570.
Article in Journal of microbiology (Seoul, Korea), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Data of crystal structure of the large Stokes shift fluorescent protein tKeima.Data in brief · 2024Article
- Structural Analysis of the Large Stokes Shift Red Fluorescent Protein tKeima.Molecules (Basel, Switzerland) · 2024Article
- Metal-Induced Fluorescence Quenching of Photoconvertible Fluorescent Protein DendFP.Molecules (Basel, Switzerland) · 2022Article
- Spectroscopic Analysis of Fe Ion-Induced Fluorescence Quenching of the Green Fluorescent Protein ZsGreen.Journal of fluorescence · 2021Article
- Spectroscopic and Structural Analysis of CuBiosensors · 2020Article
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Authors and funding
3 authors.
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Abstract
The Keima family comprises large Stokes shifts fluorescent proteins, which are useful for dual-color fluorescence crosscorrelation spectroscopy and multicolor imaging. dKeima570 belongs to the Keima family. It has a unique chromophore sequence composed of CYG with an emission peak at 570 nm, but its molecular properties are unclear. We report the spectral analysis of dKeima570 and its crystal structure at 2.0 Å resolution. The dKeima570 chromophore is mainly in the protonation state in the entire pH range. The pH-induced non-fluorescence state was observed below pH 4.0. The crystal structure of the dKeima570 chromophore has a cis conformation at pH 6.5. The chromophore is surrounded by a unique hydrogen bonding network containing a water bridge between Glu212 and Arg194. The analysis of the dimeric interface of dKeima570 revealed the key residues that maintain the oligomerization of Keima family. Structural comparisons of dKeima570 and mKeima provided insights into the unique large Stokes shifts characteristics of the Keima family.
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