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| {{STRUCTURE_2c2f| PDB=2c2f | SCENE= }} | | {{STRUCTURE_2c2f| PDB=2c2f | SCENE= }} |
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| '''DPS FROM DEINOCOCCUS RADIODURANS'''
| | ===DPS FROM DEINOCOCCUS RADIODURANS=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_16855817}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 16855817 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_16855817}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Dp]] | | [[Category: Dp]] |
| [[Category: Iron]] | | [[Category: Iron]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:08:41 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 07:21:33 2008'' |
