Solution structure and interactions of the Escherichia coli cell division activator protein CedA

Biochemistry. 2005 May 10;44(18):6738-44. doi: 10.1021/bi0500269.

Abstract

CedA is a protein that is postulated to be involved in the regulation of cell division in Escherichia coli and related organisms; however, little biological data about its possible mode of action are available. Here we present a three-dimensional structure of this protein as determined by NMR spectroscopy. The protein is made up of four antiparallel beta-strands, an alpha-helix, and a large unstructured stretch of residues at the N-terminus. It shows structural similarity to a family of DNA-binding proteins which interact with dsDNA via a three-stranded beta-sheet, suggesting that CedA may be a DNA-binding protein. The putative binding surface of CedA is predominantly positively charged with a number of basic residues surrounding a groove largely dominated by aromatic residues. NMR chemical shift perturbations and gel-shift experiments performed with CedA confirm that the protein binds dsDNA, and its interaction is mediated primarily via the beta-sheet.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs / genetics
  • Arabidopsis Proteins / chemistry
  • Arabidopsis Proteins / metabolism
  • Bacteriophage lambda / enzymology
  • Cell Cycle Proteins / chemistry*
  • Cell Cycle Proteins / metabolism*
  • Cell Cycle Proteins / physiology
  • Cell Division / physiology
  • DNA, Bacterial / chemistry
  • DNA, Bacterial / metabolism
  • DNA-Binding Proteins / chemistry*
  • DNA-Binding Proteins / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism*
  • Escherichia coli Proteins / physiology
  • Integrases / chemistry
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Peptide Termination Factors / chemistry
  • Peptide Termination Factors / metabolism
  • Protein Binding
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Solutions
  • Structural Homology, Protein
  • Surface Properties
  • Thermodynamics
  • Viral Proteins / chemistry

Substances

  • Arabidopsis Proteins
  • CedA protein, E coli
  • Cell Cycle Proteins
  • DNA, Bacterial
  • DNA-Binding Proteins
  • Escherichia coli Proteins
  • Peptide Termination Factors
  • Solutions
  • Viral Proteins
  • eukaryotic release factor 1, Arabidopsis
  • Integrases

Associated data

  • PDB/2BN8