8C05

LOV-activated diguanylate cyclase, dark-state structure

8C05 の概要

• エントリーDOI: 10.2210/pdb8c05/pdb
• 分子名称: Sensor domain-containing diguanylate cyclase, FLAVIN MONONUCLEOTIDE, DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: lov, ggdef, c-di-gmp, fmn, linker, flavoprotein
• 由来する生物種: Methylotenera sp.
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36896.69

構造登録者

Vide, U.,Winkler, A. (登録日: 2022-12-15, 公開日: 2023-07-19, 最終更新日: 2023-08-23)

主引用文献

Vide, U.,Kasapovic, D.,Fuchs, M.,Heimbock, M.P.,Totaro, M.G.,Zenzmaier, E.,Winkler, A.
Illuminating the inner workings of a natural protein switch: Blue-light sensing in LOV-activated diguanylate cyclases.
Sci Adv, 9:eadh4721-eadh4721, 2023

PubMed Abstract: Regulatory proteins play a crucial role in adaptation to environmental cues. Especially for lifestyle transitions, such as cell proliferation or apoptosis, switch-like characteristics are desirable. While nature frequently uses regulatory circuits to amplify or dampen signals, stand-alone protein switches are interesting for applications like biosensors, diagnostic tools, or optogenetics. However, such stand-alone systems frequently feature limited dynamic and operational ranges and suffer from slow response times. Here, we characterize a LOV-activated diguanylate cyclase (LadC) that offers precise temporal and spatial control of enzymatic activity with an exceptionally high dynamic range over four orders of magnitude. To establish this pronounced activation, the enzyme exhibits a two-stage activation process in which its activity is inhibited in the dark by caging its effector domains and stimulated upon illumination by the formation of an extended coiled-coil. These switch-like characteristics of the LadC system can be used to develop new optogenetic tools with tight regulation.

PubMed: 37531459
DOI: 10.1126/sciadv.adh4721

実験手法

X-RAY DIFFRACTION (2.5 Å)