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Structures of full-length VanR from Streptomyces coelicolor in both the inactive and activated states

Lina J Maciunas1, Nadia Porter1, Paula J Lee1

  • 1Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA 19102, USA.

Acta Crystallographica. Section D, Structural Biology
|August 3, 2021
PubMed

Insights

Vancomycin resistance in bacteria is controlled by the VanR-VanS system. This study reveals how VanR protein changes shape upon activation, promoting dimerization and enhancing DNA binding to trigger resistance gene expression.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Vancomycin is a critical antibiotic, but resistance is a growing public health concern.
  • Vancomycin resistance is regulated by the VanR-VanS two-component system.
  • VanR acts as a transcription factor, activating resistance genes upon phosphorylation.

Purpose of the Study:

  • To elucidate the structural mechanisms underlying VanR activation and DNA binding.
  • To provide insights into the molecular basis of vancomycin resistance.

Main Methods:

  • X-ray crystallography of full-length VanR in inactive and activated states.
  • Analytical ultracentrifugation to confirm dimerization in solution.

Main Results:

  • The crystal structures revealed a disorder-to-order transition of helix 4 in VanR upon phosphorylation.
  • This transition facilitates dimerization of the VanR receiver domain.
  • Dimerization enhances DNA binding through an avidity effect.

Conclusions:

  • Phosphorylation-induced dimerization of VanR is a key step in activating vancomycin resistance.
  • Structural insights can inform strategies to combat antibiotic resistance.
Keywords:
Streptomyces coelicolorX-ray crystallographyfull-length VanRresponse regulatorstwo-component systemsvancomycin resistance

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