5JVA

1.95 angstrom crystal structure of TAGRFP-T

「3T6H」から置き換えられました

5JVA の概要

• エントリーDOI: 10.2210/pdb5jva/pdb
• 関連するPDBエントリー: 3T6H
• 分子名称: TagRFP-T, BETA-MERCAPTOETHANOL, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: red fluorescent proteins, tagrfp-t, beta barrel, photostable, fluorescent protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 109116.31

構造登録者

Hu, X.J. (登録日: 2016-05-11, 公開日: 2017-05-17, 最終更新日: 2024-04-03)

主引用文献

Liu, R.,Liang, Q.N.,Du, S.Q.,Hu, X.J.,Ding, Y.
The crystal structure of red fluorescent protein TagRFP-T reveals the mechanism of its superior photostability.
Biochem. Biophys. Res. Commun., 477:229-234, 2016

PubMed Abstract: The red fluorescent protein variant TagRFP-T has greatly improved photostability over its parent molecule, TagRFP, but the underlying mechanism leading to this improvement is to date unknown. The 1.95 Å resolution crystallographic structure of TagRFP-T showed that its chromophore exists as a mixture of cis and trans coplanar isomers in roughly equal proportions. Interestingly, both isomers are able to fluoresce, a property that has never been observed in any other fluorescent protein. We propose a "circular restoration model" for TagRFP-T to explain its superior photostability: There are four co-existing chromophore states (cis/trans protonated/ionized state) that can be driven by light to transform from one state into another. This model also explains how TagRPF-T essentially eliminates the temporary dark state (reversible photobleaching).

PubMed: 27297107
DOI: 10.1016/j.bbrc.2016.06.047

実験手法

X-RAY DIFFRACTION (1.95 Å)