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.
Zaveer
M Shahzad
MS
Chemistry Department, Connecticut College, 270 Mohegan Avenue, New London, CT 06320, USA.
Zimmer
Marc
M
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