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TitleTrans-cis isomerization is responsible for the red-shifted fluorescence in variants of the red fluorescent protein eqFP611.
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 130, Page 12578-12579, Year 2008
Publish dateAug 14, 2008 (structure data deposition date)
AuthorsNienhaus, K. / Nar, H. / Heilker, R. / Wiedenmann, J. / Nienhaus, G.U.
External linksJ. Am. Chem. Soc. / PubMed:18761441
MethodsX-ray diffraction
Resolution1.1 - 2.1 Å
Structure data

PDB-3e5t:
Crystal Structure Analysis of FP611
Method: X-RAY DIFFRACTION / Resolution: 1.1 Å

PDB-3e5v:
Crystal Structure Analysis of eqFP611 Double Mutant T122R, N143S
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3e5w:
Crystal Structure Analysis of FP611
Method: X-RAY DIFFRACTION / Resolution: 1.71 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • entacmaea quadricolor (sea anemone)
KeywordsFLUORESCENT PROTEIN / Chromophore / Luminescence / Photoprotein / red fluorescent protein / d2RFP630 / cis-trans isomer / RFP639 / eqFP611 / cis trans isomer

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