2C2U

Dps from Deinococcus radiodurans

Summary for 2C2U

• Entry DOI: 10.2210/pdb2c2u/pdb
• Related: 2C2F
• Descriptor: DNA-BINDING STRESS RESPONSE PROTEIN, SULFATE ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: dna-binding protein, dps, iron, deinococcus radiodurans, dna-binding, dna binding protein
• Biological source: DEINOCOCCUS RADIODURANS
• Cellular location: Cytoplasm, nucleoid (By similarity): Q9RS64
• Total number of polymer chains: 1
• Total formula weight: 23268.04

Authors

Romao, C.V.,Mitchell, E.,McSweeney, S. (deposition date: 2005-09-30, release date: 2006-07-26, Last modification date: 2023-12-13)

Primary citation

Romao, C.V.,Mitchell, E.,Mcsweeney, S.
The Crystal Structure of Deinococcus Radiodurans Dps Protein (Dr2263) Reveals the Presence of a Novel Metal Centre in the N Terminus.
J.Biol.Inorg.Chem., 11:891-, 2006

PubMed Abstract: 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 ferroxidase centre with structural similarities to those found in other Dps family members; the two other sites are located on the two different threefold axes corresponding to small pores in the Dps sphere, which may possibly form the entrance and exit channels for iron storage.

PubMed: 16855817
DOI: 10.1007/S00775-006-0142-5

Experimental method

X-RAY DIFFRACTION (1.1 Å)