2XGW

ZINC-BOUND CRYSTAL STRUCTURE OF STREPTOCOCCUS PYOGENES DPR

Summary for 2XGW

• Entry DOI: 10.2210/pdb2xgw/pdb
• Descriptor: PEROXIDE RESISTANCE PROTEIN, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: metal binding protein
• Biological source: STREPTOCOCCUS PYOGENES
• Total number of polymer chains: 1
• Total formula weight: 22500.61

Authors

Haikarainen, T.,Tsou, C.-C.,Wu, J.-J.,Papageorgiou, A.C. (deposition date: 2010-06-08, release date: 2010-08-11, Last modification date: 2024-05-08)

Primary citation

Haikarainen, T.,Tsou, C.-C.,Wu, J.-J.,Papageorgiou, A.C.
Structural Characterization and Biological Implications of Di-Zinc Binding in the Ferroxidase Center of Streptococcus Pyogenes Dpr.
Biochem.Biophys.Res.Commun., 398:361-, 2010

PubMed Abstract: Dps 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.

PubMed: 20599728
DOI: 10.1016/J.BBRC.2010.06.071

Experimental method

X-RAY DIFFRACTION (2.1 Å)