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Related Concept Videos

Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
Allosteric Regulation01:08

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 Regulation01:08

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...
Ligand Binding and Linkage00:49

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 Transitions01:58

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 Transitions01:58

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...

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Updated: Jun 28, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
08:00

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

Published on: October 4, 2024

Surface sites for engineering allosteric control in proteins.

Jeeyeon Lee1, Madhusudan Natarajan, Vishal C Nashine

  • 1Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.

Science (New York, N.Y.)
|October 18, 2008
PubMed
Summary
This summary is machine-generated.

Scientists engineered a new protein, PAS-DHFR, by linking a light-sensing domain with an enzyme. This creates a controllable protein that responds to light, demonstrating a new method for protein engineering.

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Area of Science:

  • Biochemistry
  • Protein Engineering
  • Molecular Biology

Background:

  • Protein families exhibit coevolving amino acid networks linking distant functional surfaces.
  • These networks suggest a strategy for engineering allosteric control into proteins by joining intramolecular networks.

Purpose of the Study:

  • To test the concept of engineering allosteric control by creating a chimeric protein.
  • To demonstrate that protein activity can be regulated by connecting signaling domains to enzymes.

Main Methods:

  • Statistical analysis of protein families to identify coevolving amino acid networks.
  • Design and creation of a chimeric protein (PAS-DHFR) by fusing a plant Per/Arnt/Sim (PAS) signaling domain with Escherichia coli dihydrofolate reductase (DHFR).

Main Results:

  • The designed PAS-DHFR chimeric protein exhibited light-dependent catalytic activity without optimization.
  • The observed light-dependent activity was contingent on the specific connection site and known signaling mechanisms of both parent proteins.

Conclusions:

  • PAS-DHFR serves as a proof of concept for engineering regulatory functions into proteins.
  • Interface design at conserved allosteric sites is a viable strategy for creating novel regulatory activities in proteins.