PMID:15865419
| Citation |
Chen, HA, Simpson, P, Huyton, T, Roper, D and Matthews, S (2005) Solution structure and interactions of the Escherichia coli cell division activator protein CedA. Biochemistry 44:6738-44 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1021/bi0500269 |
| Keywords |
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 |
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