2XGW

ZINC-BOUND CRYSTAL STRUCTURE OF STREPTOCOCCUS PYOGENES DPR

2XGW の概要

• エントリーDOI: 10.2210/pdb2xgw/pdb
• 分子名称: PEROXIDE RESISTANCE PROTEIN, ZINC ION, CHLORIDE ION, ... (6 entities in total)
• 機能のキーワード: metal binding protein
• 由来する生物種: STREPTOCOCCUS PYOGENES
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 22500.61

構造登録者

Haikarainen, T.,Tsou, C.-C.,Wu, J.-J.,Papageorgiou, A.C. (登録日: 2010-06-08, 公開日: 2010-08-11, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)