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Spatiotemporal Control of Protein Activity through Optogenetic Allosteric Regulation
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Probing allosteric regulations with coevolution-driven molecular simulations.

Francesco Colizzi1, Modesto Orozco1,2

  • 1Institute for Research in Biomedicine (IRB Barcelona), Barcelona Institute of Science and Technology (BIST), Carrer de Baldiri Reixac 10, Barcelona 08028, Spain.

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|September 13, 2021
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Summary
This summary is machine-generated.

Researchers quantified protein allosteric regulation using computational methods. The study reveals a simple ON/OFF switch mechanism for adenylyl cyclase (AC) regulation by G proteins, advancing our understanding of biomolecular signaling.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Computational Biology

Background:

  • Protein-mediated allosteric regulation is crucial for biological processes.
  • Quantitative characterization of these regulations presents significant experimental and computational challenges.

Purpose of the Study:

  • To develop and apply a computational approach for quantifying allosteric regulation in protein complexes.
  • To investigate the molecular mechanisms underlying adenylyl cyclase (AC) regulation by stimulatory and inhibitory G proteins.

Main Methods:

  • Integration of coevolutionary information, multiscale molecular simulations, and free-energy calculations.
  • Application to the adenylyl cyclase-G protein system.

Main Results:

  • Revealed a simple ON/OFF switch governing AC functional dynamics.
  • Demonstrated that G protein binding reshapes the AC free-energy landscape via a population-shift mechanism.
  • Identified novel, experimentally consistent intermediate states.

Conclusions:

  • The developed computational strategy provides a general method for exploring complex biomolecular regulations.
  • The findings offer new insights into the allosteric regulation of adenylyl cyclase by G proteins.