8C05

LOV-activated diguanylate cyclase, dark-state structure

Summary for 8C05

• Entry DOI: 10.2210/pdb8c05/pdb
• Descriptor: Sensor domain-containing diguanylate cyclase, FLAVIN MONONUCLEOTIDE, DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: lov, ggdef, c-di-gmp, fmn, linker, flavoprotein
• Biological source: Methylotenera sp.
• Total number of polymer chains: 1
• Total formula weight: 36896.69

Authors

Vide, U.,Winkler, A. (deposition date: 2022-12-15, release date: 2023-07-19, Last modification date: 2023-08-23)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)