کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1392534 | 983750 | 2010 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Structural Characterization of Acylimine-Containing Blue and Red Chromophores in mTagBFP and TagRFP Fluorescent Proteins Structural Characterization of Acylimine-Containing Blue and Red Chromophores in mTagBFP and TagRFP Fluorescent Proteins](/preview/png/1392534.png)
SummaryWe determined the 2.2 Å crystal structures of the red fluorescent protein TagRFP and its derivative, the blue fluorescent protein mTagBFP. The crystallographic analysis is consistent with a model in which TagRFP has the trans coplanar anionic chromophore with the conjugated π-electron system, similar to that of DsRed-like chromophores. Refined conformation of mTagBFP suggests the presence of an N-acylimine functionality in its chromophore and single Cα-Cβ bond in the Tyr64 side chain. Mass spectrum of mTagBFP chromophore-bearing peptide indicates a loss of 20 Da upon maturation, whereas tandem mass spectrometry reveals that the Cα-N bond in Leu63 is oxidized. These data indicate that mTagBFP has a new type of the chromophore, N-[(5-hydroxy-1H-imidazole-2-yl)methylidene]acetamide. We propose a chemical mechanism in which the DsRed-like chromophore is formed via the mTagBFP-like blue intermediate.
Graphical AbstractFigure optionsDownload high-quality image (171 K)Download as PowerPoint slideHighlights
► Crystal structure of the brightest monomeric red fluorescent protein TagRFP
► Crystal structure of the first blue fluorescent protein mTagBFP with tyrosine
► Chemical structure of a novel blue chromophore having the acylimine group
► Mechanism of formation of the DsRed-like red chromophore via a blue intermediate
Journal: - Volume 17, Issue 4, 23 April 2010, Pages 333–341