9C74

superfolder Green Fluorescent Protein with meta-nitro-tyrosine incorporated at position 66

9C74 の概要

• エントリーDOI: 10.2210/pdb9c74/pdb
• 関連するPDBエントリー: 6UN6
• 分子名称: Green fluorescent protein, SODIUM ION (3 entities in total)
• 機能のキーワード: nitrotyrosine, gfp, sfgfp, uaa, ncaa, fluorescent protein
• 由来する生物種: Aequorea victoria
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27127.41

構造登録者

Phillips-Piro, C.M.,Broughton, D.P. (登録日: 2024-06-10, 公開日: 2024-10-16, 最終更新日: 2026-03-18)

主引用文献

Broughton, D.P.,Holod, C.G.,Camilo-Contreras, A.,Harris, D.R.,Brewer, S.H.,Phillips-Piro, C.M.
Modulating the pH dependent photophysical properties of green fluorescent protein.
Rsc Adv, 14:32284-32291, 2024

PubMed Abstract: The photophysical properties of the β-barrel superfolder green fluorescent protein (sfGFP) arise from the chromophore that forms post-translationally in the interior of the protein. Specifically, the protonation state of the side chain of tyrosine 66 in the chromophore, in addition to the network of hydrogen bonds between the chromophore and surrounding residues, is directly related to the electronic absorbance and emission properties of the protein. The pH dependence of the photophysical properties of this protein were modulated by the genetic, site-specific incorporation of 3-nitro-l-tyrosine (mNOY) at site 66 in sfGFP. The altered photophysical properties of this noncanonical amino acid (ncAA) sfGFP construct were assessed by absorbance and fluorescence spectroscopies. Notably, a comparison of the p of the 3-nitrophenol side chain of mNOY incorporated in the protein relative to the phenol side chain of the tyrosine at site 66 in the native chromophore as well as the p of the 3-nitrophenol side chain of the free ncAA were measured and are compared. A structural analysis of the ncAA containing sfGFP construct is presented to yield molecular insight into the origin of the altered absorbance and fluorescence properties of the protein.

PubMed: 39421683
DOI: 10.1039/d4ra05058d

実験手法

X-RAY DIFFRACTION (1.51 Å)