- Spectral and structural analysis of large Stokes shift fluorescent protein dKeima570
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Yongbin Xu , Kwang Yeon Hwang , Ki Hyun Nam
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J. Microbiol. 2018;56(11):822-827. Published online October 24, 2018
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DOI: https://doi.org/10.1007/s12275-018-8319-5
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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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