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

Ho An Chen, Peter Simpson, Trevor Huyton, David Roper, Stephen Matthews

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4 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)6738 - 6744
Number of pages7
JournalBiochemistry
Volume44
Issue number18
DOIs
Publication statusPublished - 2005

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