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Related Concept Videos

Allosteric Regulation01:08

Allosteric Regulation

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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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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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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...
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Cellular needs and conditions vary from cell to cell and change within individual cells over time. For example, the required enzymes and energetic demands of stomach cells are different from those of fat storage cells, skin cells, blood cells, and nerve cells. Furthermore, a digestive cell works much harder to process and break down nutrients during the time that closely follows a meal compared with many hours after a meal. As these cellular demands and conditions vary, so do the amounts and...
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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Engineering allosteric communication.

Zachary D Herde1, Andrew E Short1, Valerie E Kay1

  • 1Georgia Institute of Technology, School of Chemical & Biomolecular Engineering, United States.

Current Opinion in Structural Biology
|June 24, 2020
PubMed
Summary
This summary is machine-generated.

Understanding protein allostery remains challenging. Engineering LacI proteins offers insights into designing allosteric communication, paving the way for predictive protein design.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Protein Engineering

Background:

  • Protein allostery is crucial for cellular functions but difficult to understand at a molecular level.
  • Allosteric communication is a key feature in many proteins, yet its mechanisms are still under investigation after decades of research.

Purpose of the Study:

  • To review recent advances in understanding and engineering protein allosteric communication.
  • To explore the prerequisites for the de novo design of allosteric pathways.
  • To highlight progress towards predictive design of allosteric systems based on protein topology.

Main Methods:

  • Engineering of the LacI protein and its homologues to introduce novel allosteric communication pathways.
  • Analysis of structural and functional data to identify key features enabling allosteric regulation.
  • Review of current literature on protein allostery and de novo design strategies.

Main Results:

  • Engineering efforts have provided insights into the requirements for creating allosteric communication.
  • Specific modifications to LacI have demonstrated the feasibility of altering allosteric pathways.
  • While complete de novo design of allosteric pathways has not yet been achieved, significant progress has been made.

Conclusions:

  • Recent advancements in protein engineering and allostery research are laying the groundwork for predictive design.
  • Understanding the fundamental principles of allosteric communication is key to engineering novel protein functions.
  • Future research aims to achieve the de novo design of functional allosteric pathways for specific protein topologies.