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Allosteric movements in eubacterial RecA.

Anu V Chandran1, M Vijayan2

  • 1Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560012, India.

Biophysical Reviews
|May 17, 2017
PubMed
Summary
This summary is machine-generated.

RecA protein transitions from inactive to active states via DNA and ATP binding. Structural studies reveal a switch residue and C-terminal ordering crucial for RecA

Keywords:
Correlated intra-molecular movementsDNA and nucleotide bindingMolecular plasticityMycobacterial RecARecombination and repair

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Area of Science:

  • Structural biology
  • Molecular biology
  • Eubacterial protein function

Background:

  • RecA protein mediates DNA recombination and repair.
  • Its function involves a transition from inactive to active filament states.
  • Previous studies characterized RecA interactions with nucleotides and DNA binding loops.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying RecA activation.
  • To identify key residues and regions involved in RecA's allosteric transitions.
  • To characterize the role of the C-terminal stretch in RecA function.

Main Methods:

  • X-ray crystallography of RecA proteins (EcRecA, MtRecA, MsRecA) and mutants.
  • Complex formation with DNA, ATP analogues, ADP, and dATP.
  • Analysis of crystal structures under varying conditions (temperature, humidity).

Main Results:

  • Visualized DNA binding loops and characterized nucleotide interactions.
  • Identified a switch residue triggering conformational changes.
  • Defined the ordered C-terminal stretch in an MsRecA-dATP complex, revealing a new nucleotide binding site.
  • Observed correlated movements in RecA structures linked to allosteric transitions.

Conclusions:

  • The switch residue and ordered C-terminal stretch are critical for RecA's allosteric regulation.
  • Correlated movements across RecA molecules facilitate its functional transitions.
  • Structural insights advance understanding of DNA repair and recombination mechanisms.