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Related Experiment Videos

A common dimerization interface in bacterial response regulators KdpE and TorR.

Alejandro Toro-Roman1, Ti Wu, Ann M Stock

  • 1Center for Advanced Biotechnology and Medicine, 679 Hoes Lane, Piscataway, NJ 08854, USA.

Protein Science : a Publication of the Protein Society
|December 3, 2005
PubMed
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Bacterial response regulators activate through dimerization. This study confirms a common activation mechanism for the OmpR/PhoB subfamily of response regulators, involving conserved residues.

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Microbiology

Background:

  • Bacterial response regulators are crucial proteins in two-component signaling systems.
  • Their activity is modulated by phosphorylation, controlled by histidine protein kinases sensing external signals.

Purpose of the Study:

  • To investigate the activation mechanism of the OmpR/PhoB subfamily of response regulators.
  • To provide structural evidence for a hypothesized common dimerization mechanism.

Main Methods:

  • X-ray crystallography was used to determine the structures of TorR and KdpE regulatory domains.
  • Structures were solved at high resolution (1.8-2.2 A) for different binding states.

Main Results:

  • The regulatory domains of TorR and KdpE (both OmpR/PhoB subfamily) form symmetric dimers.

Related Experiment Videos

  • Dimerization interfaces involve conserved residues on the alpha4-beta5-alpha5 face.
  • Structural data support a common dimerization-based activation mechanism for this subfamily.

    • Conclusions:

    • The OmpR/PhoB subfamily of response regulators likely shares a common activation mechanism involving dimerization.
    • Conserved residues mediate the dimerization interface, suggesting evolutionary conservation of this activation strategy.