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Structural Protein Function

Structural Protein Function

Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin.
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Structural Protein Function

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Protein and Protein Structure

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G-protein Coupled Receptors

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G Protein-coupled Receptors

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Mechanical Protein Functions

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Related Experiment Video

Updated: Jan 30, 2026

Imaging G Protein-coupled Receptor-mediated Chemotaxis and its Signaling Events in Neutrophil-like HL60 Cells

Imaging G Protein-coupled Receptor-mediated Chemotaxis and its Signaling Events in Neutrophil-like HL60 Cells

Published on: September 14, 2016

Bacterial chemotaxis coupling protein: Structure, function and diversity.

Zhiwei Huang¹, Xiaoyue Pan¹, Nan Xu¹

¹College of Bioscience and Biotechnology, Yangzhou University, PR China.

Microbiological Research

|January 16, 2019

Summary

Bacterial chemotaxis uses coupling proteins like CheW and CheV to link receptors and histidine kinases for signal transduction. This review details their structures, functions, and diverse roles in forming chemosensory arrays.

Keywords:

Chemoreceptor Core signaling complex Protein interaction Protein phosphorylation Signal transduction

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Imaging G-protein Coupled Receptor GPCR-mediated Signaling Events that Control Chemotaxis of Dictyostelium Discoideum

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A Microfluidic Device for Quantifying Bacterial Chemotaxis in Stable Concentration Gradients

A Microfluidic Device for Quantifying Bacterial Chemotaxis in Stable Concentration Gradients

Published on: April 19, 2010

Area of Science:

Microbiology
Molecular Biology
Biochemistry

Background:

Signal transduction systems rely on coupling or scaffold proteins to connect receptors and histidine kinases.
The bacterial chemotaxis system is a well-studied model for signal transduction, utilizing specific coupling proteins.
Chemotaxis involves methyl-accepting chemotaxis proteins (MCPs) and histidine kinase CheA.

Purpose of the Study:

To summarize the molecular mechanism of chemotaxis in Escherichia coli.
To review recent advances in the structural details and functions of CheW and CheV coupling proteins.
To discuss the diversity and relationships of multiple coupling proteins within an organism.

Main Methods:

Literature review of molecular mechanisms in bacterial chemotaxis.
Analysis of structural and functional data for CheW and CheV.
Comparative study of coupling protein diversity.

Main Results:

CheW and CheV are the two main architectures of coupling proteins in chemotaxis.
CheW bridges histidine kinase CheA dimers and chemoreceptor trimers of dimers to form signaling complexes.
CheW also facilitates the formation of large chemosensory arrays for signal amplification, while CheV has partially redundant but distinct functions.

Conclusions:

CheW and CheV play critical roles in bacterial chemotaxis signal transduction.
Understanding the structural and functional diversity of these coupling proteins is key to comprehending chemotaxis.
Further research into the interplay of multiple coupling proteins can reveal complex signaling networks.