2bn8
From Proteopedia
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SOLUTION STRUCTURE AND INTERACTIONS OF THE E.COLI CELL DIVISION ACTIVATOR PROTEIN CEDA
Overview
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.
About this Structure
2BN8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Solution structure and interactions of the Escherichia coli cell division activator protein CedA., Chen HA, Simpson P, Huyton T, Roper D, Matthews S, Biochemistry. 2005 May 10;44(18):6738-44. PMID:15865419
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