The structural basis for red fluorescence in the tetrameric GFP homolog DsRed

M. A. Wall, M. Socolich, R. Ranganathan

Research output: Contribution to journalArticlepeer-review

294 Scopus citations

Abstract

Green fluorescent protein (GFP) has rapidly become a standard tool for investigating a variety of cellular activities, and has served as a model system for understanding spectral tuning in chromophoric proteins. Distant homologs of GFP in reef coral and anemone display two new properties of the fluorescent protein family: dramatically red-shifted spectra, and oligomerization to form tetramers. We now report the 1.9 Å crystal structure of DsRed, a red fluorescent protein from Discosoma coral. DsRed monomers show similar topology to GFP, but additional chemical modification to the chromophore extends the conjugated π-system and likely accounts for the red-shifted spectra. Oligomerization of DsRed occurs at two chemically distinct protein interfaces to assemble the tetramer. The DsRed structure reveals the chemical basis for the functional properties of red fluorescent proteins and provides the basis for rational engineering of this subfamily of GFP homologs.

Original languageEnglish (US)
Pages (from-to)1133-1138
Number of pages6
JournalNature Structural Biology
Volume7
Issue number12
DOIs
StatePublished - 2000

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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