2c2u
DPS FROM DEINOCOCCUS RADIODURANS
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OverviewOverview
The crystal structure of a DNA-binding protein from starved cells (Dps), (DR2263) from Deinococcus radiodurans was determined in two states: a, native form, to 1.1-A resolution, and one soaked in an iron solution, to, 1.6-A resolution. In comparison with other Dps proteins, DR2263 has an, extended N-terminal extension, in both structures presented here, a novel, metal binding site was identified in this N-terminal extension and was, assigned to bound zinc. The zinc is tetrahedrally coordinated and the, ligands, that belong to the N-terminal extension, are two histidines, one, glutamate and one aspartate residue, which are unique to this protein, within the Dps family. In the iron-soaked crystal structure, a total of, three iron sites per monomer were found: one site corresponds to the, ... [(full description)]
About this StructureAbout this Structure
2C2U is a [Single protein] structure of sequence from [Deinococcus radiodurans] with SO4, ZN and FE as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus., Romao CV, Mitchell EP, McSweeney S, J Biol Inorg Chem. 2006 Oct;11(7):891-902. Epub 2006 Jul 20. PMID:16855817
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