A1 Refereed original research article in a scientific journal
Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr
Authors: Haikarainen T, Tsou CC, Wu JJ, Papageorgiou AC
Publisher: ACADEMIC PRESS INC ELSEVIER SCIENCE
Publication year: 2010
Journal: Biochemical and Biophysical Research Communications
Journal name in source: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Journal acronym: BIOCHEM BIOPH RES CO
Volume: 398
Issue: 3
First page : 361
Last page: 365
Number of pages: 5
ISSN: 0006-291X
DOI: https://doi.org/10.1016/j.bbrc.2010.06.071
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. (C) 2010 Elsevier Inc. All rights reserved.
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. (C) 2010 Elsevier Inc. All rights reserved.
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