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Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

Ligand Binding and Linkage

Ligand Binding and Linkage

Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence the...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...

Allosteric Regulation

Allosteric Regulation

Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...

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Related Experiment Video

Updated: Jul 15, 2026

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

Published on: August 17, 2022

Ligand binding and allostery can emerge simultaneously.

Jing Liang¹, Jin Ryoun Kim, Jason T Boock

¹Program in Molecular and Computational Biophysics, Johns Hopkins University, Baltimore, Maryland 21218, USA.

Protein Science : a Publication of the Protein Society

|April 3, 2007

Summary

Researchers engineered enzymes with novel allosteric regulation. They discovered a new zinc-binding site that controls enzyme activity, offering insights into how allosteric effects evolve.

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Visualizing the Conformational Dynamics of Membrane Receptors Using Single-Molecule FRET

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Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library

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Published on: January 14, 2020

Area of Science:

Biochemistry
Molecular Biology
Enzyme Engineering

Background:

Heterotropic allostery, where effector molecules differ from substrates, lacks a clear origin explanation.
Previous work created chimeric enzymes combining TEM1 beta-lactamase (BLA) and maltose binding protein (MBP) for maltose-regulated allostery.

Purpose of the Study:

Investigate the origin and mechanisms of heterotropic allostery.
Characterize a novel allosteric enzyme engineered from BLA and MBP.

Main Methods:

Enzyme engineering by gene recombination (BLA and MBP).
Biochemical assays to determine enzyme kinetics and effector binding.
Site-directed mutagenesis to identify key residues and structural elements.

Main Results:

Engineered enzyme exhibits significant affinity (10^6 M^-1) for Zn(2+), a property absent in parent proteins.
Zn(2+) acts as a noncompetitive inhibitor, reducing beta-lactam hydrolysis activity.
Mutagenesis suggests Zn(2+) binding involves atypical residues and implicates BLA helices 1 and 12 in allosteric signal transmission.

Conclusions:

The findings support a model where effector binding and allosteric signaling co-evolve.
This study provides a novel mechanism for heterotropic allostery emergence.