4KGE

Crystal structure of near-infrared fluorescent protein with an extended stokes shift, pH 4.5

4KGE の概要

• エントリーDOI: 10.2210/pdb4kge/pdb
• 関連するPDBエントリー: 4KGF
• 分子名称: TagRFP675, red fluorescent protein, CHLORIDE ION (3 entities in total)
• 機能のキーワード: structural genomics, proteinstructure initiative, new york structural genomix researchconsortium, hydrolase, psi-biology, new york structural genomics research consortium, nysgrc, fluorescent protein
• 由来する生物種: synthetic construct (artificial gene)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 55701.71

構造登録者

Malashkevich, V.N.,Piatkevich, K.,Almo, S.C.,Verkhusha, V.,New York Structural Genomics Research Consortium (NYSGRC) (登録日: 2013-04-29, 公開日: 2013-05-08, 最終更新日: 2023-12-06)

主引用文献

Piatkevich, K.D.,Malashkevich, V.N.,Morozova, K.S.,Nemkovich, N.A.,Almo, S.C.,Verkhusha, V.V.
Extended Stokes shift in fluorescent proteins: chromophore-protein interactions in a near-infrared TagRFP675 variant.
Sci Rep, 3:1847-1847, 2013

PubMed Abstract: Most GFP-like fluorescent proteins exhibit small Stokes shifts (10-45 nm) due to rigidity of the chromophore environment that excludes non-fluorescent relaxation to a ground state. An unusual near-infrared derivative of the red fluorescent protein mKate, named TagRFP675, exhibits the Stokes shift, which is 30 nm extended comparing to that of the parental protein. In physiological conditions, TagRFP675 absorbs at 598 nm and emits at 675 nm that makes it the most red-shifted protein of the GFP-like protein family. In addition, its emission maximum strongly depends on the excitation wavelength. Structures of TagRFP675 revealed the common DsRed-like chromophore, which, however, interacts with the protein matrix via an extensive network of hydrogen bonds capable of large flexibility. Based on the spectroscopic, biochemical, and structural analysis we suggest that the rearrangement of the hydrogen bond interactions between the chromophore and the protein matrix is responsible for the TagRFP675 spectral properties.

PubMed: 23677204
DOI: 10.1038/srep01847

実験手法

X-RAY DIFFRACTION (2.3 Å)