title: Solution structure and interactions of the Escherichia coli cell division activator protein CedA.
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.
authors.affiliation: Department of Biological Sciences and Centre for Structural Biology, Imperial College of Science, Technology and Medicine, South Kensington, London, UK.
authors.forename: Ho An
authors.initials: HA
authors.lastname: Chen
authors.forename: Peter
authors.initials: P
authors.lastname: Simpson
authors.forename: Trevor
authors.initials: T
authors.lastname: Huyton
authors.forename: David
authors.initials: D
authors.lastname: Roper
authors.forename: Stephen
authors.initials: S
authors.lastname: Matthews
mesh_terms: D020816:Amino Acid Motifs / Q000235:genetics; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000378:metabolism; D010582:Bacteriophage lambda / Q000201:enzymology; D018797:Cell Cycle Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D002455:Cell Division / Q000502:physiology; D004269:DNA, Bacterial / Q000737:chemistry / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism* / Q000502:physiology; D019426:Integrases / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010454:Peptide Termination Factors / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012996:Solutions; D040681:Structural Homology, Protein; D013499:Surface Properties; D013816:Thermodynamics; D014764:Viral Proteins / Q000737:chemistry
chemical_list: D029681:Arabidopsis Proteins; C110342:CedA protein, E coli; D018797:Cell Cycle Proteins; D004269:DNA, Bacterial; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D010454:Peptide Termination Factors; D012996:Solutions; D014764:Viral Proteins; C494978:eukaryotic release factor 1, Arabidopsis; D019426:Integrases