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Related Concept Videos

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

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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

Protein function and allostery: a dynamic relationship.

Charalampos G Kalodimos1

  • 1Department of Chemistry and Chemical Biology, Rutgers University, Piscataway, New Jersey, USA. babis@rutgers.edu

Annals of the New York Academy of Sciences
|January 20, 2012
PubMed
Summary

Allosteric regulation, crucial for biological processes, can be driven by protein motion changes, not just structural shifts. This finding redefines our understanding of how proteins communicate and are activated.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Allostery is a fundamental biological mechanism regulating protein activity across diverse processes.
  • Recent advancements, particularly in nuclear magnetic resonance (NMR) spectroscopy, have enhanced our understanding of allosteric principles.
  • Nuclear magnetic resonance spectroscopy provides atomic-level insights into protein dynamics.

Purpose of the Study:

  • To discuss recent findings on the catabolite activator protein (CAP) that reshape the understanding of allosteric modulation.
  • To highlight novel mechanisms of allosteric regulation revealed by studies on CAP.

Main Methods:

  • Utilized nuclear magnetic resonance (NMR) spectroscopy to investigate protein dynamics.
  • Analyzed allosteric regulation in the catabolite activator protein (CAP).

Main Results:

  • Demonstrated that allostery can be mediated by alterations in protein intrinsic motions, independent of changes in mean protein structure.
  • Identified that favorable changes in protein motions can activate allosteric proteins that are structurally inactive.
  • CAP serves as the first experimentally validated system exhibiting these novel allosteric mechanisms.

Conclusions:

  • Allosteric regulation is not solely dependent on structural changes but can be driven by dynamic motion modulation.
  • Protein dynamics play a critical role in allosteric activation, offering new perspectives on protein function and regulation.
  • These findings necessitate a revised framework for understanding allosteric mechanisms in biological systems.