Three-dimensional structure of a pH-dependent fluorescent protein WasCFP with a tryptophan based deprotonated chromophore

V. Z. Pletnev, N. V. Pletneva, R. G. Efremov, E. A. Goryacheva, I. V. Artemyev, S. F. Arkhipova, K. S. Sarkisyan, A. S. Mishin, K. A. Lukyanov, S. V. Pletnev

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

WasCFP, a pH-dependent green fluorescent protein with a tryptophan-based chromophore (Thr65-Trp66-Gly67) in anionic state, was designed from a cyan precursor mCerulean. In this study, the three-dimensional structure of WasCFP has been determined by an X-ray method at pH 5.5, pH 8.0 and pH 10.0, with a resolution of 1.14, 1.25 and 1.5 Å, respectively. We show that changes in the acidity of the media are accompanied by a synchronous change of the side chain conformations of the residues in the near-chromophore environment. Subsequent changes in the local H-bond network interacting with the chromophore lead to considerable alterations in the protein spectral properties as a consequence of reversible processes of ionization-protonation of the Trp chromophore. These experimental results have been supported by quantum chemistry calculations.

Original languageEnglish
Pages (from-to)612-618
Number of pages7
JournalRussian Journal of Bioorganic Chemistry
Volume42
Issue number6
DOIs
Publication statusPublished - 1 Nov 2016
Externally publishedYes

Keywords

  • crystal structure
  • green fluorescent protein WasCFP
  • Trp anionic form
  • Trp based chromophore

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