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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...

Allosteric Regulation

Allosteric Regulation

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...

Cooperative Allosteric Transitions

Cooperative Allosteric Transitions

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

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Related Experiment Video

Updated: Apr 22, 2026

Author Spotlight: Advancing Tendon Research by Developing Mouse Assembloids to Understand Cellular Mechanisms

Author Spotlight: Advancing Tendon Research by Developing Mouse Assembloids to Understand Cellular Mechanisms

Published on: March 22, 2024

Engineering allostery.

Srivatsan Raman¹, Noah Taylor¹, Naomi Genuth¹

¹Wyss Institute for Biologically-Inspired Engineering, Harvard University, 3 Blackfan Circle, Boston, MA 02115, USA; Department of Genetics, Harvard Medical School, 77 Avenue Louis Pasteur, Boston, MA 02115, USA.

Trends in Genetics : TIG

|October 13, 2014

Summary

This summary is machine-generated.

This study presents a new method to identify key sites for allostery in proteins like LacI. This advance aids in designing novel synthetic biology tools for gene regulation.

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Area of Science:

Synthetic Biology
Molecular Biology
Protein Engineering

Background:

Allosteric proteins are crucial for synthetic biology but understanding their molecular mechanisms remains limited.
This limits the development of designer molecules like transcription factors with tailored DNA-binding or ligand-binding properties.
Allosteric proteins could serve as switches, sensors, or orthogonal regulators in complex biological circuits.

Purpose of the Study:

To develop a method for identifying critical residues involved in protein allostery.
To facilitate the engineering of allosteric proteins for synthetic biology applications.
To gain mechanistic insights into allosteric regulation.

Main Methods:

Developed a genetic selection system utilizing a bidirectional reporter.
Applied the system to the LacI protein to capture mutants in both allosteric states.
Leveraged advances in DNA synthesis and next-generation sequencing for high-throughput mutant assessment.

Main Results:

Successfully identified key positions crucial for allostery in the LacI protein.
Demonstrated the utility of the bidirectional reporter system for studying allosteric mutants.
Validated the approach for uncovering essential residues in protein allosteric regulation.

Conclusions:

The described genetic selection system enables identification of critical allosteric sites.
This methodology can be applied beyond bacterial transcription factors to engineer diverse allosteric proteins.
Facilitates the creation of novel synthetic biology tools with predictable allosteric responses.