Crystal structures of Staphylococcal SaeR reveal possible DNA-binding modes

Biochem Biophys Res Commun. 2016 Jun 10;474(4):686-690. doi: 10.1016/j.bbrc.2016.05.009. Epub 2016 May 3.

Abstract

Two-component system SaeRS of Staphylococcus regulates virulence factor expression through phosphorylation of the DNA-binding regulator SaeR by the sensor histidine kinase SaeS. Here crystal structures of the DNA-binding domain (DBD) of SaeR from two Staphylococcal species Staphylococcus epidermidis and Staphylococcus aureus were determined and showed similar folds. Analyzing the DNA binding activity of three mutants of SeSaeR, we observed that Thr217 is important in binding to the phosphate group of DNA and Trp219 may interact with the base pairs. Additionally, the tandem arrangement of DBD may represent a possible way for SaeR oligomerization on DNA.

Keywords: Crystal structure; SaeR; Staphylococcus; Two-component system.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / ultrastructure*
  • Binding Sites
  • Computer Simulation
  • Crystallography / methods
  • DNA, Bacterial / chemistry*
  • DNA, Bacterial / ultrastructure*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / ultrastructure
  • Models, Chemical
  • Models, Molecular
  • Protein Binding
  • Protein Conformation
  • Structure-Activity Relationship
  • Transcription Factors

Substances

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