Structural analysis of the immature form of the GFP homologue DsRed.
The crystal structures of DsRed have shown that it contains an unusual non-proline containing cis peptide linkage. We have shown that it is also present in the precyclized immature form of DsRed, thereby eliminating the possibility that cis/trans isomerization drives the formation of the acylimine, which is responsible for DsRed's red fluorescence. Two mechanisms have been proposed for chromophore formation in green fluorescent protein (GFP), a "reduced" and an "oxidized" mechanism. DsRed adopts a tight turn conformation, such as that found in GFP, in the immature intermediate proposed in the oxidized mechanism, but not in the one predicted by the reduced mechanism.
Chemistry Department, Connecticut College, 270 Mohegan Avenue, New London, CT 06320, USA.
M Shahzad
MS
Zaveer
Marc
M
Zimmer
D018360:Crystallography, X-Ray; D004151:Dipeptides / Q000737:chemistry; D005973:Glutamine; D049452:Green Fluorescent Proteins; D008164:Luminescent Proteins / Q000737:chemistry*; D010649:Phenylalanine; D011487:Protein Conformation
D004151:Dipeptides; D008164:Luminescent Proteins; C413663:fluorescent protein 583; D005973:Glutamine; D049452:Green Fluorescent Proteins; D010649:Phenylalanine