Structural highlights
Function
C3YRA2_BRAFL
Publication Abstract from PubMed
We describe an engineered violet fluorescent protein from the lancelet Branchiostoma floridae (bfVFP). This is the first example of a GFP-like fluorescent protein with a stable fluorescent chromophore lacking an imidazolinone ring; instead, it consists of oxidized tyrosine 68 flanked by glycine 67 and alanine 69. bfVFP contains the simplest chromophore reported in fluorescent proteins and was generated from the yellow protein lanFP10A2 by two synergetic mutations, S148H and C166I. The chromophore structure was confirmed crystallographically and by high-resolution mass spectrometry. The photophysical characteristics of bfVFP (323/430 nm, quantum yield 0.33, and Ec 14,300 M(-1) cm(-1) ) make it potentially useful for multicolor experiments to expand the excitation range of available FP biomarkers and Forster resonance energy transfer with blue and cyan fluorescent protein acceptors.
A novel violet fluorescent protein contains a unique oxidized tyrosine as the simplest chromophore ever reported in fluorescent proteins.,Roldan-Salgado A, Muslinkina L, Pletnev S, Pletneva N, Pletnev V, Gaytan P Protein Sci. 2022 Mar;31(3):688-700. doi: 10.1002/pro.4265. Epub 2022 Jan 3. PMID:34936154[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Roldán-Salgado A, Muslinkina L, Pletnev S, Pletneva N, Pletnev V, Gaytán P. A novel violet fluorescent protein contains a unique oxidized tyrosine as the simplest chromophore ever reported in fluorescent proteins. Protein Sci. 2022 Mar;31(3):688-700. PMID:34936154 doi:10.1002/pro.4265
