What is it about?
We report here the X-ray structures of the intact NowGFP at pH 9.0 and pH 4.8, and of its photoconverted variant, NowGFP_conv, at 1.35, 1.18, and 2.5Å resolution, respectively. The structure of NowGFP at pH 9.0 suggests the anionic state of Trp66 of the chromophore to be the primary cause of its green fluorescence. At both examined pH, Trp66 predominantly adopts cis conformation; only ~20% of trans conformation was observed at pH 4.8. It was shown that Lys61 is a key residue, playing a central role in the chromophore indole ring ionization.
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Why is it important?
Direction for design new biomarkers,
Perspectives
We hope this paper will initiate the experiments on design new gene engineering variants of fluorescent proteins based on Trp.
Vladimir Pletnev
Read the Original
This page is a summary of: NowGFP: a green fluorescent protein with an anionic tryptophan-based chromophore, Acta Crystallographica Section A Foundations and Advances, August 2015, International Union of Crystallography,
DOI: 10.1107/s2053273315097004.
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