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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,...
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...
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...
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...

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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation

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Light-activated DNA binding in a designed allosteric protein.

Devin Strickland1, Keith Moffat, Tobin R Sosnick

  • 1Department of Biochemistry and Molecular Biology and Institute for Biophysical Dynamics, University of Chicago, 929 East 57th Street, Chicago, IL 60637, USA.

Proceedings of the National Academy of Sciences of the United States of America
|August 1, 2008
PubMed
Summary
This summary is machine-generated.

Researchers engineered a protein fusion to control DNA binding using light. This demonstrates a general helical "allosteric lever arm" strategy for protein communication in signaling networks and protein design.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Engineering

Background:

  • Allostery, the regulation of protein function through conformational changes distant from the active site, is crucial in biological systems.
  • Understanding the mechanisms of allostery in evolvable systems is key for cell biology, protein design, and signaling network research.

Purpose of the Study:

  • To investigate the potential of a rigid alpha-helical domain linker as a conduit for allosteric signals.
  • To rationally design and test protein fusions for light-inducible allosteric control.

Main Methods:

  • Rational design of 12 fusion proteins combining the LOV2 domain (from Avena sativa phototropin 1) and the Escherichia coli trp repressor.
  • Illumination experiments to assess the functional properties of the designed fusions, including DNA binding and protection from nuclease digestion.

Main Results:

  • One designed fusion protein exhibited light-dependent, selective binding to operator DNA.
  • The illuminated fusion protein successfully protected operator DNA from nuclease digestion, indicating functional allosteric control.
  • The success validates the helical "allosteric lever arm" as an effective design strategy.

Conclusions:

  • A helical linker can effectively mediate allosteric signals between protein domains.
  • This rational design approach provides a generalizable method for creating light-switchable protein systems.
  • The findings have implications for protein design, synthetic biology, and understanding biological signaling.