2OTE

Crystal structure of a monomeric cyan fluorescent protein in the photobleached state

2OTE の概要

• エントリーDOI: 10.2210/pdb2ote/pdb
• 関連するPDBエントリー: 2OTB
• 分子名称: GFP-like fluorescent chromoprotein cFP484, ACETATE ION (3 entities in total)
• 機能のキーワード: beta can, fluorescent protein
• 由来する生物種: Clavularia sp.
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 49657.42

構造登録者

Henderson, J.N.,Ai, H.,Campbell, R.E.,Remington, S.J. (登録日: 2007-02-07, 公開日: 2007-04-03, 最終更新日: 2023-11-15)

主引用文献

Henderson, J.N.,Ai, H.W.,Campbell, R.E.,Remington, S.J.
Structural basis for reversible photobleaching of a green fluorescent protein homologue.
Proc.Natl.Acad.Sci.Usa, 104:6672-6677, 2007

PubMed Abstract: Fluorescent protein (FP) variants that can be reversibly converted between fluorescent and nonfluorescent states have proven to be a catalyst for innovation in the field of fluorescence microscopy. However, the structural basis of the process remains poorly understood. High-resolution structures of a FP derived from Clavularia in both the fluorescent and the light-induced nonfluorescent states reveal that the rapid and complete loss of fluorescence observed upon illumination with 450-nm light results from cis-trans isomerization of the chromophore. The photoinduced change in configuration from the well ordered cis isomer to the highly nonplanar and disordered trans isomer is accompanied by a dramatic rearrangement of internal side chains. Taken together, the structures provide an explanation for the loss of fluorescence upon illumination, the slow light-independent recovery, and the rapid light-induced recovery of fluorescence. The fundamental mechanism appears to be common to all of the photoactivatable and reversibly photoswitchable FPs reported to date.

PubMed: 17420458
DOI: 10.1073/pnas.0700059104

実験手法

X-RAY DIFFRACTION (1.47 Å)