1umn
From Proteopedia
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CRYSTAL STRUCTURE OF DPS-LIKE PEROXIDE RESISTANCE PROTEIN (DPR) FROM STREPTOCOCCUS SUIS
Overview
The Dps-like peroxide resistance protein (Dpr) is an aerotolerance and, hydrogen peroxide resistance agent found in the meningitis-associated, pathogen Streptococcus suis. Dpr is believed to act by binding free, intracellular iron to prevent Fenton chemistry-catalysed formation of, toxic hydroxyl radicals. The crystal structure of Dpr has been determined, to 1.95 A resolution. The final model has an Rcyst value of 18.5% (Rfree =, 22.4%) and consists of 12 identical monomers (each of them comprising a, four alpha-helix bundle) that form a hollow sphere obeying 23 symmetry., Structural features show that Dpr belongs to the Dps family of bacterial, proteins. Twelve putative ferroxidase centers, each formed at the, interface of neighboring monomer pairs, were identified in the Dpr, structure ... [(full description)]
About this Structure
1UMN is a [Single protein] structure of sequence from [Streptococcus suis] with CA, CL and EPE as [ligands]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation., Kauko A, Haataja S, Pulliainen AT, Finne J, Papageorgiou AC, J Mol Biol. 2004 Apr 30;338(3):547-58. PMID:15081812
Page seeded by OCA on Mon Oct 29 22:02:01 2007
Categories: Single protein | Streptococcus suis | Finne, J. | Haataja, S. | Kauko, A. | Papageorgiou, A.C. | Pulliainen, A. | CA | CL | EPE | Dps-family | Ferritin-like | Ferroxidase | Iron-binding | Peroxide resistance
