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Related Experiment Video

Updated: Jan 7, 2026

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

Published on: December 12, 2017

Bacterial Chemoreceptors Transmit Stimulus Signals Through Coupled Entropic Switches.

Caralyn E Flack¹, John S Parkinson¹

¹School of Biological Sciences, University of Utah, Salt Lake City, UT 84112, United States.

Journal of Molecular Biology

|December 25, 2025

Summary

This summary is machine-generated.

Signal transduction in bacterial chemoreceptors involves conformational changes. This study reveals how these changes propagate through the Tsr receptor, identifying key "entropic switches" that control kinase output.

Keywords:

chemotaxis protein crosslinking signal transduction

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Area of Science:

Microbiology
Molecular Biology
Biochemistry

Background:

Transmembrane sensory proteins mediate signal transduction by undergoing conformational changes upon ligand binding.
Understanding these dynamic structural alterations is crucial for deciphering cellular communication pathways.
Bacterial chemoreceptors, like Tsr, are model systems for studying stimulus-response coupling.

Purpose of the Study:

To investigate the propagation of conformational changes within the cytoplasmic signaling domain of the bacterial chemoreceptor Tsr.
To identify the structural mechanisms underlying kinase output control in Tsr.
To explore the role of specific amino acid substitutions in modulating receptor dynamics and function.

Main Methods:

Engineering of mutant Tsr receptors with amino acid replacements to lock kinase activity in ON or OFF states.
In vivo assays including crosslinking for structural analysis and kinase activity measurements for functional assessment.
Utilizing AlphaFold 3 to generate atomic models of mutant receptors and analyze predicted structural changes.

Main Results:

Conformational changes initiated at mutation sites propagated bidirectionally throughout the Tsr signaling domain without significant dissipation.
These propagation behaviors were intrinsic to Tsr homodimers and independent of larger signaling complexes.
AlphaFold 3 models revealed that mutations altered helix packing, with some reducing and others enhancing local stability, pinpointing two
entropic switches
in the signaling pathway.

Conclusions:

Chemoreceptor signaling involves dynamic switches, with kinase-OFF mutations showing differential stability effects across the cytoplasmic domain.
The findings provide new insights into the mechanism of kinase output control and conformational coupling in transmembrane receptors.
The study highlights the synergistic potential of combining experimental cellular signaling data with computational modeling (AlphaFold 3) for protein structure-function analysis.