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2bw1
From Proteopedia
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IRON-BOUND CRYSTAL STRUCTURE OF DPS-LIKE PEROXIDE RESISTANCE PROTEIN (DPR) FROM STREPTOCOCCUS SUIS.
Overview
The Dps-like peroxide resistance protein (Dpr) is a dodecameric protein, that protects the human and swine pathogen Streptococcus suis from, hydrogen peroxide by removing free Fe2+ from the cytosol. Subsequent, oxidation of iron by Dpr results in the deposition of Fe3+ inside the, protein's central cavity. Structural changes that occur in the ferroxidase, center were studied by X-ray crystallography after soaking Dpr crystals, with Fe2+ in the presence of sodium dithionite. Twelve iron-binding sites, were identified with each site formed by residues Asp74 and Glu78 from one, subunit, and Asp63, His47 and His59 from a 2-fold symmetry-related, subunit. Compared to the iron-free Dpr, Asp74 and Glu78 were found to be, the most flexible amino acid residues and able to adopt a variety of, ... [(full description)]
About this Structure
2BW1 is a [Single protein] structure of sequence from [Streptococcus suis] with FE, CA and EPE as [ligands]. Structure known Active Site: FEA. Full crystallographic information is available from [OCA].
Reference
Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to the formation of a ferrihydrite-like core., Kauko A, Pulliainen AT, Haataja S, Meyer-Klaucke W, Finne J, Papageorgiou AC, J Mol Biol. 2006 Nov 17;364(1):97-109. Epub 2006 Aug 26. PMID:16997323
Page seeded by OCA on Tue Oct 30 16:49:40 2007
Categories: Single protein | Streptococcus suis | Finne, J. | Haataja, S. | Kauko, A. | Papageorgiou, A.C. | Pulliainen, A. | CA | EPE | FE | Dpr | Dps-family | Ferritin-like | Ferroxidase | Iron-binding | Peroxide resistance
