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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,...
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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of the...
tRNA Activation02:26

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Aminoacyl-tRNA synthetases are present in both eukaryotes and bacteria. Though eukaryotes have 20 different aminoacyl-tRNA synthetases to couple to 20 amino acids, many bacteria do not have genes for all of these aminoacyl-tRNA synthetases. Despite this, they still use all 20 amino acids to synthesize their proteins. For instance, some bacteria do not have the gene encoding the enzyme that couples glutamine with its partner tRNA. In these organisms, one enzyme adds glutamic acid to all of 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...
Cooperative Allosteric Transitions01:58

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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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Related Experiment Video

Updated: May 26, 2026

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
11:47

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

An exclusive α/β code directs allostery in TetR-peptide complexes.

Madhumati Sevvana1, Christoph Goetz, Dagmar Goeke

  • 1Lehrstuhl für Biotechnik, Department of Biology, Friedrich-Alexander University Erlangen-Nuremberg, Henkestr. 91, D-91052 Erlangen, Germany.

Journal of Molecular Biology
|December 20, 2011
PubMed
Summary

Synthetic peptides reveal that the tetracycline repressor (TetR) likely functions via a classical two-state allosteric model, challenging previous cooperative folding hypotheses for this bacterial transcription regulator.

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Related Experiment Videos

Last Updated: May 26, 2026

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System
11:47

Residue-specific Incorporation of Noncanonical Amino Acids into Model Proteins Using an Escherichia coli Cell-free Transcription-translation System

Published on: August 1, 2016

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Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction
11:02

Genetic Encoding of a Non-Canonical Amino Acid for the Generation of Antibody-Drug Conjugates Through a Fast Bioorthogonal Reaction

Published on: September 14, 2018

Area of Science:

  • Molecular Biology
  • Protein Dynamics
  • Biochemistry

Background:

  • The allosteric mechanism of the bacterial transcription regulator, tetracycline repressor (TetR), is under scrutiny.
  • Recent studies suggest TetR undergoes cooperative folding upon tetracycline binding, rather than conformational switching.

Purpose of the Study:

  • To investigate TetR's allosteric mechanism using synthetic peptides that mimic effector molecules.
  • To differentiate between proposed allosteric models for TetR function.

Main Methods:

  • Structure-function studies using four synthetic peptides designed to interact with TetR.
  • Analysis of peptide conformations (β-like vs. α-helical) within the TetR effector binding site.
  • Urea-induced unfolding studies and fluorescence measurements to assess protein stability and binding.

Main Results:

  • Two inducing peptides adopted a β-like conformation, while two anti-inducing peptides formed an α-helix.
  • These distinct binding modes correlated with two specific TetR conformations, one resembling induced TetR and the other the DNA-bound state.
  • No increase in thermodynamic stability was observed for peptide-TetR complexes, despite confirmed peptide binding.

Conclusions:

  • The bimodal interaction of peptides with TetR supports a classical two-state allosteric model.
  • This finding challenges the cooperative folding model for TetR, particularly for these peptide effectors.