2C6R
FE-SOAKED CRYSTAL STRUCTURE OF THE DPS92 FROM DEINOCOCCUS RADIODURANS
Summary for 2C6R
| Entry DOI | 10.2210/pdb2c6r/pdb |
| Related | 2C2J |
| Descriptor | DNA-BINDING STRESS RESPONSE PROTEIN, DPS FAMILY, FE (III) ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | dps, deinococcus, radiodurans, dna-binding protein, dna binding protein |
| Biological source | DEINOCOCCUS RADIODURANS |
| Cellular location | Cytoplasm (By similarity): Q9RZN1 |
| Total number of polymer chains | 1 |
| Total formula weight | 23604.39 |
| Authors | Cuypers, M.G.,Romao, C.V.,Mitchell, E.,Mcsweeney, S. (deposition date: 2005-11-11, release date: 2007-02-20, Last modification date: 2024-05-08) |
| Primary citation | Cuypers, M.G.,Mitchell, E.P.,Romao, C.V.,Mcsweeney, S.M. The Crystal Structure of the Dps2 from Deinococcus Radiodurans Reveals an Unusual Pore Profile with a Non-Specific Metal Binding Site. J.Mol.Biol., 371:787-, 2007 Cited by PubMed Abstract: The crystal structure of recombinant Dps2 (DRB0092, DNA protecting protein under starved conditions) from the Gram-positive, radiation-resistant bacterium Deinococcus radiodurans has been determined in its apo and iron loaded states. Like other members of the Dps family, the bacterial DrDps2 assembles as a spherical dodecamer with an outer shell diameter of 90 A and an interior diameter of 40 A. A total of five iron sites were located in the iron loaded structure, representing the first stages of iron biomineralisation. Each subunit contains a mononuclear iron ferroxidase centre coordinated by residues highly conserved amongst the Dps family of proteins. In the structures presented, a distinct iron site is observed 6.1 A from the ferroxidase centre with a unique ligand configuration of mono coordination by the protein and no bridging ligand to the ferroxidase centre. A non-specific metallic binding site, suspected to play a regulative role in iron uptake/release from the cage, was found in a pocket located near to the external edge of the C-terminal 3-fold channel. PubMed: 17583727DOI: 10.1016/J.JMB.2006.11.032 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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