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ZINC-BOUND CRYSTAL STRUCTURE OF STREPTOCOCCUS PYOGENES DPRZINC-BOUND CRYSTAL STRUCTURE OF STREPTOCOCCUS PYOGENES DPR
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDps proteins contain a ferroxidase site that binds and oxidizes iron, thereby preventing hydroxyl radical formation by Fenton reaction. Although the involvement of a di-iron ferroxidase site has been suggested, X-ray crystal structures of various Dps members have shown either one or two iron cations with various occupancies despite the high structural conservation of the site. Similarly, structural studies with zinc, a redox-stable replacement for iron, have shown the binding of either one or two zinc ions. Here, the crystal structure of Streptococcus pyogenes Dpr in complex with zinc reveals the binding of two zinc cations in the ferroxidase center and an additional zinc-binding site at the surface of the protein. The results suggest a structural basis for the protection of Streptococcus pyogenes in zinc stress conditions and provide a clear evidence for a di-zinc and di-iron ferroxidase site in Streptococcus pyogenes Dpr protein. Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr.,Haikarainen T, Tsou CC, Wu JJ, Papageorgiou AC Biochem Biophys Res Commun. 2010 Jul 30;398(3):361-5. Epub 2010 Jun 19. PMID:20599728[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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