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Allosteric Regulation01:08

Allosteric Regulation

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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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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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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...
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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...
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Sensing the allosteric force.

Olga Bozovic1, Brankica Jankovic1, Peter Hamm2

  • 1Department of Chemistry, University of Zurich, Zurich, Switzerland.

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|November 18, 2020
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Summary
This summary is machine-generated.

Researchers engineered a protein system to observe allosteric regulation, demonstrating how a photoswitch controls protein-ligand binding affinity and ligand binding influences the photoswitch. This work introduces an "allosteric force" concept for driving chemical reactions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Allosteric regulation is crucial for cellular adaptation, modulating protein activity and binding affinity.
  • Understanding allosteric mechanisms at a molecular level is key to deciphering complex biological pathways.

Purpose of the Study:

  • To design and investigate a protein system enabling bidirectional observation of allosteric communication.
  • To explore the relationship between photoswitch isomerization, protein-ligand binding, and allosteric effects.

Main Methods:

  • Engineered a PDZ3 protein domain system incorporating an azobenzene photoswitch on the α3-helix.
  • Utilized photo-induced trans-to-cis isomerization of the photoswitch to modulate ligand binding affinity.
  • Analyzed the system's energetics across four states (cis/trans, ligand-bound/free) to define an allosteric force.

Main Results:

  • Photoisomerization of the azobenzene switch increased peptide ligand binding affinity to the PDZ3 domain by up to 120-fold.
  • Ligand binding accelerated the thermal cis-to-trans back-isomerization of the photoswitch.
  • Established a quantitative framework for allosteric force based on system energetics.

Conclusions:

  • The designed system provides a microscopic view of bidirectional allosteric communication.
  • Photoswitchable allosteric control of protein-ligand interactions is feasible and highly tunable.
  • The concept of allosteric force offers a novel perspective for controlling molecular processes and driving reactions.