2BN8

Solution Structure and interactions of the E .coli Cell Division Activator Protein CedA

Summary for 2BN8

• Entry DOI: 10.2210/pdb2bn8/pdb
• NMR Information: BMRB: 5950
• Descriptor: CELL DIVISION ACTIVATOR CEDA (1 entity in total)
• Functional Keywords: ceda, cell division activator protein, cell cycle protein
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 1
• Total formula weight: 10215.90

Authors

Chen, H.A.,Simpson, P.,Huyton, T.,Roper, D.,Matthews, S. (deposition date: 2005-03-22, release date: 2006-12-21, Last modification date: 2024-05-15)

Primary citation

Chen, H.A.,Simpson, P.,Huyton, T.,Roper, D.,Matthews, S.
Solution Structure and Interactions of the Escherichia Coli Cell Division Activator Protein Ceda.
Biochemistry, 44:6738-, 2005

PubMed 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.

PubMed: 15865419
DOI: 10.1021/BI0500269

Experimental method

SOLUTION NMR