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Method for Efficient Refolding and Purification of Chemoreceptor Ligand Binding Domain

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Published on: December 12, 2017

Flexible Hinges in Bacterial Chemoreceptors.

Narahari Akkaladevi¹, Filiz Bunyak², David Stalla³

¹Department of Biochemistry, University of Missouri, Columbia, Missouri, USA.

Journal of Bacteriology

|December 13, 2017

Summary

Bacterial chemoreceptors, essential for chemotaxis, possess flexible hinges allowing bending. This structural flexibility prevents clashes, enabling the formation of signaling complexes and chemoreceptor arrays.

Keywords:

bacterial chemotaxis helical coiled coils protein arrays transmembrane proteins transmembrane signaling

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Area of Science:

Structural biology
Microbiology
Biophysics

Background:

Transmembrane bacterial chemoreceptors form homodimers crucial for chemotaxis.
Existing structural data lacks intact, membrane-inserted receptor information, showing heterogeneity in signaling arrays.

Purpose of the Study:

To characterize the molecular shape of intact, functional homodimers of the *Escherichia coli* aspartate receptor Tar.
To investigate the structural basis for heterogeneity observed in chemoreceptor arrays.

Main Methods:

Negative staining transmission electron microscopy (TEM).
Single-particle analysis and cryo-electron tomography of chemoreceptors in nanodisc lipid bilayers.
Image analysis to determine 3D structures and identify bend loci.

Main Results:

Identified two flexible hinge regions in the cytoplasmic domain of Tar chemoreceptors.
Observed variable bending (0-13° at HAMP domain, 0-20° at glycine-rich region) at these hinges.
Demonstrated that hinge bending avoids steric clashes, facilitating signaling complex and array formation.

Conclusions:

Intact *E. coli* Tar chemoreceptors exhibit flexible hinges, explaining structural heterogeneity in arrays.
Hinge flexibility is crucial for proper assembly of chemotaxis signaling complexes, independent of signaling state.