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2bw1

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[[Category: peroxide resistance]]
[[Category: peroxide resistance]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 11:04:27 2007''
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 16:49:40 2007''

Revision as of 14:44, 30 October 2007

Image:2bw1.gif

2bw1, resolution 1.81Å

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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

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