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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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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.
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The two-state receptor model explains a drug's interaction with receptors, such as G protein-coupled receptors and ligand-gated ion channels, to induce or inhibit a biological response. When no natural ligands are present, a receptor exists in an equilibrium of inactive (Ri) and active (Ra) conformations. The inactive form does not produce a response, while the active form generates a basal effect known as constitutive activity.
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Mixed, nonclassical behavior in a classic allosteric protein.

Paul J Sapienza1, Jeffrey P Bonin2, H P Dinusha Jinasena1

  • 1Division of Chemical Biology and Medicinal Chemistry, Eshelman School of Pharmacy, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599.

Proceedings of the National Academy of Sciences of the United States of America
|September 11, 2023
PubMed
Summary
This summary is machine-generated.

Allostery in yeast chorismate mutase (CM) involves uncoupled subunit switching, challenging classic models. This dynamic behavior, observed via NMR, reveals a shift to a high-energy state, not the typical relaxed state, under specific conditions.

Keywords:
AllosteryMWCNMR dynamicsensemble allosteric modelrelaxation dispersion

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Allostery regulates biological processes through conformational changes.
  • Classic models describe allostery using T (tense) and R (relaxed) states.
  • Understanding allosteric mechanisms is crucial for biological process manipulation.

Purpose of the Study:

  • To investigate the dynamic allosteric mechanism of yeast chorismate mutase (CM).
  • To challenge and refine existing phenomenological models of allostery.
  • To explore the role of dynamic ensembles in allosteric regulation.

Main Methods:

  • Methyl-based Nuclear Magnetic Resonance (NMR) spectroscopy.
  • Analysis of allosteric protein dynamics.
  • Characterization of enzyme conformational states.

Main Results:

  • Observed uncoupled switching of individual subunits in dimeric CM.
  • Directly visualized mixed T-R states, excluding classic models.
  • Identified a switch to a high-energy state, not the R state, in the apo enzyme.
  • NMR structures of activator-bound and effector-free CM were indistinguishable, highlighting dynamic ensembles.

Conclusions:

  • Classic allosteric models are insufficient to explain CM behavior.
  • Allosteric regulation involves dynamic conformational ensembles.
  • The allosteric mechanism of CM adapts to different allosteric inputs, suggesting context-dependent models.