1o9r
THE X-RAY CRYSTAL STRUCTURE OF AGROBACTERIUM TUMEFACIENS DPS, A MEMBER OF THE FAMILY THAT PROTECT DNA WITHOUT BINDING
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OverviewOverview
Agrobacterium tumefaciens Dps (DNA-binding proteins from starved cells), encoded by the dps gene located on the circular chromosome of this plant, pathogen, was cloned, and its structural and functional properties were, determined in vitro. In Escherichia coli Dps, the family prototype, the, DNA binding properties are thought to be associated with the presence of, the lysine-containing N-terminal tail that extends from the protein, surface into the solvent. The x-ray crystal structure of A. tumefaciens, Dps shows that the positively charged N-terminal tail, which is 11 amino, acids shorter than in the E. coli protein, is blocked onto the protein, surface. This feature accounts for the lack of interaction with DNA. The, intersubunit ferroxidase center characteristic of Dps proteins is, ... [(full description)]
About this StructureAbout this Structure
1O9R is a [Single protein] structure of sequence from [Agrobacterium tumefaciens] with FE, TRS and EDO as [ligands]. Full crystallographic information is available from [OCA].
ReferenceReference
The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: x-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties., Ceci P, Ilari A, Falvo E, Chiancone E, J Biol Chem. 2003 May 30;278(22):20319-26. Epub 2003 Mar 26. PMID:12660233
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