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Related Concept Videos

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...
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 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

Allosteric control in a metalloprotein dramatically alters function.

Elizabeth Leigh Baxter1, John A Zuris, Charles Wang

  • 1Department of Chemistry and Biochemistry and Center for Theoretical Biological Physics, University of California at San Diego, La Jolla, CA 92093, USA.

Proceedings of the National Academy of Sciences of the United States of America
|December 29, 2012
PubMed
Summary
This summary is machine-generated.

Metalloproteins, which are crucial for biological chemistry, can be regulated by distant protein regions. A specific loop in mitoNEET allosterically controls its metal center, impacting function without structural changes.

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Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

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Last Updated: May 15, 2026

Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Published on: October 4, 2024

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
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Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS

Published on: April 13, 2016

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR
14:44

Structure and Coordination Determination of Peptide-metal Complexes Using 1D and 2D 1H NMR

Published on: December 16, 2013

Area of Science:

  • Biochemistry and Structural Biology
  • Metalloprotein research
  • Protein dynamics and allostery

Background:

  • Metalloproteins (MPs) constitute a significant portion of known protein structures, utilizing inorganic moieties for unique chemical functions.
  • Traditionally, MPs are considered rigid, with metal center properties attributed solely to the immediate amino acid environment.
  • The diabetes drug target mitoNEET is a key metalloprotein whose regulatory mechanisms are under investigation.

Purpose of the Study:

  • To investigate whether distal regions of metalloproteins can influence the metal center.
  • To examine the allosteric control exerted by a distant loop (L2) on the metal center of mitoNEET.
  • To understand the functional implications of long-range dynamical changes in metalloprotein backbones.

Main Methods:

  • Theoretical and experimental examinations of the mitoNEET protein.
  • Mutagenesis of the L2 loop to assess its impact on the [2Fe-2S] cluster.
  • All-atom simulations to analyze native basin dynamics and protein backbone movements.

Main Results:

  • A loop (L2), 20 Å from the metal center, was found to exert allosteric control over mitoNEET's cluster binding domain.
  • Mutagenesis of L2 significantly altered the redox potential of the [2Fe-2S] cluster and cluster transfer rates.
  • These functional changes occurred without observable structural alterations, driven by dynamical changes in L2 affecting coordinating histidines.

Conclusions:

  • Distal regions, specifically the L2 loop in mitoNEET, can allosterically regulate metalloprotein function.
  • Long-range protein backbone dynamics play a critical role in modulating the properties and function of metalloprotein metal centers.
  • Findings challenge the traditional view of metalloprotein rigidity and highlight the importance of protein dynamics in biological chemistry.