9EBX

Chimeric fluorescence biosensor formed from a lactate-binding protein and GFP

9EBX の概要

• エントリーDOI: 10.2210/pdb9ebx/pdb
• 関連するPDBエントリー: 9EBW
• 分子名称: Green fluorescent protein,Methyl-accepting chemotaxis transducer (TlpC) (2 entities in total)
• 機能のキーワード: biosensor, binding protein, chimera, fluorescent protein
• 由来する生物種: Aequorea victoria; 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58440.97

構造登録者

Horwitz, S.M.,Ambarian, J.A.,Waidmann, L.,Davis, K.M. (登録日: 2024-11-13, 公開日: 2025-03-19)

主引用文献

Rosen, P.C.,Horwitz, S.M.,Brooks, D.J.,Kim, E.,Ambarian, J.A.,Waidmann, L.,Davis, K.M.,Yellen, G.
State-dependent motion of a genetically encoded fluorescent biosensor.
Proc.Natl.Acad.Sci.USA, 122:e2426324122-e2426324122, 2025

PubMed Abstract: Genetically encoded biosensors can measure biochemical properties such as small-molecule concentrations with single-cell resolution, even in vivo. Despite their utility, these sensors are "black boxes": Very little is known about the structures of their low- and high-fluorescence states or what features are required to transition between them. We used LiLac, a lactate biosensor with a quantitative fluorescence-lifetime readout, as a model system to address these questions. X-ray crystal structures and engineered high-affinity metal bridges demonstrate that LiLac exhibits a large interdomain twist motion that pulls the fluorescent protein away from a "sealed," high-lifetime state in the absence of lactate to a "cracked," low-lifetime state in its presence. Understanding the structures and dynamics of LiLac will help to think about and engineer other fluorescent biosensors.

PubMed: 40048274
DOI: 10.1073/pnas.2426324122

実験手法

X-RAY DIFFRACTION (2.42 Å)