Crystallization and preliminary X-ray diffraction analysis of the DNA-binding domain of the response regulator SaeR from Staphylococcus epidermidis

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jun;69(Pt 6):689-91. doi: 10.1107/S1744309113012943. Epub 2013 May 25.

Abstract

SaeR is the response regulator of the SaeRS two-component signal transduction system, which is involved in regulating bacterial autolysis and biofilm formation. SaeR comprises an N-terminal receiver domain and a C-terminal effector domain. The effector domain possesses DNA-binding and transactivation functions. Here, the effector domain of SaeR from Staphylococcus epidermidis was purified and crystallized using the sitting-drop vapour-diffusion method. The crystals diffracted to a resolution of 2.15 Å and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 34.20, b = 53.78, c = 111.66 Å. Determining the structure will provide insights into the mechanisms underlying DNA binding.

Keywords: SaeR; Staphylococcus epidermidis; two-component systems.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallization
  • DNA, Bacterial / chemistry*
  • DNA, Bacterial / metabolism
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / metabolism
  • Protein Binding / physiology
  • Protein Structure, Tertiary
  • Staphylococcus epidermidis*
  • Transcription Factors
  • X-Ray Diffraction

Substances

  • Bacterial Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • SaeR protein, Staphylococcus aureus
  • Transcription Factors