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Updated: Jan 20, 2026

Single-Strand DNA Binding SSB Proteins
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Agrobacterial, Single-Stranded DNA-Binding Protein VirE2 and Its Complexes.

Yury Gusev1, Svyatoslav Mazilov1, Irina Volokhina1

  • 1Bioengineering Laboratory, Institute of Biochemistry and Physiology of Plants and Microorganisms, Russian Academy of Sciences, Saratov, Russia.

Journal of Computational Biology : a Journal of Computational Molecular Cell Biology
|September 6, 2019
PubMed
Summary
This summary is machine-generated.

Agrobacterium tumefaciens VirE2 protein binds single-stranded DNA (ssDNA) and forms dimers and tetramers. Computational methods revealed disordered protein regions are key to forming these ssDNA-VirE2 complexes.

Keywords:
ssDNAssDNA-binding protein VirE2supramolecular complexes

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Structural Biology

Background:

  • VirE2 from Agrobacterium tumefaciens is crucial for transferring single-stranded DNA (ssDNA) into eukaryotic cells.
  • The protein's N- and C-termini are presumed disordered, influencing its function.

Purpose of the Study:

  • To investigate the structural dynamics and ssDNA-binding interactions of VirE2.
  • To explore the formation and implications of VirE2 oligomers (dimers and tetramers) in complex with ssDNA.

Main Methods:

  • X-ray diffraction was used to study the crystallized portion of VirE2.
  • Computational methods, including molecular dynamics simulations and in silico complex modeling, were employed.
  • The Platinum program was utilized to analyze surface properties of VirE2 complexes.

Main Results:

  • Molecular dynamics simulations showed no significant domain reorientation in VirE2 without VirE1.
  • In silico studies demonstrated the formation of ssDNA-VirE2 complexes, including dimers and tetramers.
  • Disordered protein regions were implicated in the formation of these multi-subunit complexes.

Conclusions:

  • VirE2 can form dimers and tetramers in complex with ssDNA, facilitated by its disordered termini.
  • Hydrophilic amino acids dominate the surface of the four-subunit VirE2 complex, suggesting roles in ssDNA interaction or stability.