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000097456 0247_ $$2pmid$$apmid:20599728
000097456 0247_ $$2doi$$a10.1016/j.bbrc.2010.06.071
000097456 0247_ $$2ISSN$$a1090-2104
000097456 0247_ $$2ISSN$$a0006-291X
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000097456 1001_ $$aHaikarainen, T.
000097456 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000097456 245__ $$aStructural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr.
000097456 260__ $$aOrlando, Fla.$$bAcademic Press$$c2010
000097456 300__ $$a361-365
000097456 3367_ $$00$$2EndNote$$aJournal Article
000097456 3367_ $$2BibTeX$$aARTICLE
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000097456 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000097456 440_0 $$0PERI:(DE-600)1461396-7$$aBiochem. Biophys. Res. Commun.$$v398$$x0006-291X$$y3
000097456 500__ $$3Converted on 2013-05-30 15:51
000097456 500__ $$3Converted on 2013-06-21 19:21
000097456 520__ $$aDps proteins contain a ferroxidase site that binds and oxidizes iron, thereby preventing hydroxyl radical formation by Fenton reaction. Although the involvement of a di-iron ferroxidase site has been suggested, X-ray crystal structures of various Dps members have shown either one or two iron cations with various occupancies despite the high structural conservation of the site. Similarly, structural studies with zinc, a redox-stable replacement for iron, have shown the binding of either one or two zinc ions. Here, the crystal structure of Streptococcus pyogenes Dpr in complex with zinc reveals the binding of two zinc cations in the ferroxidase center and an additional zinc-binding site at the surface of the protein. The results suggest a structural basis for the protection of Streptococcus pyogenes in zinc stress conditions and provide a clear evidence for a di-zinc and di-iron ferroxidase site in Streptococcus pyogenes Dpr protein.
000097456 536__ $$0G:(DE-H253)POF2-K1.2-20130405$$aDORIS Beamline K1.2 (POF2-54G13)$$cPOF2-54G13$$fPOF II$$x0
000097456 588__ $$aDataset connected to Pubmed
000097456 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000097456 650_2 $$2MeSH$$aBacterial Proteins: genetics
000097456 650_2 $$2MeSH$$aBinding Sites
000097456 650_2 $$2MeSH$$aCeruloplasmin: chemistry
000097456 650_2 $$2MeSH$$aCeruloplasmin: genetics
000097456 650_2 $$2MeSH$$aCrystallography, X-Ray
000097456 650_2 $$2MeSH$$aDNA-Binding Proteins: chemistry
000097456 650_2 $$2MeSH$$aDNA-Binding Proteins: genetics
000097456 650_2 $$2MeSH$$aProtein Conformation
000097456 650_2 $$2MeSH$$aStreptococcus pyogenes: enzymology
000097456 650_2 $$2MeSH$$aZinc: chemistry
000097456 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000097456 650_7 $$00$$2NLM Chemicals$$aDNA-Binding Proteins
000097456 650_7 $$00$$2NLM Chemicals$$aDpr protein, Streptococcus
000097456 650_7 $$07440-66-6$$2NLM Chemicals$$aZinc
000097456 650_7 $$0EC 1.16.3.1$$2NLM Chemicals$$aCeruloplasmin
000097456 693__ $$0EXP:(DE-H253)D-K1.2-20150101$$1EXP:(DE-H253)DORISIII-20150101$$6EXP:(DE-H253)D-K1.2-20150101$$aDORIS III$$fDORIS Beamline K1.2$$x0
000097456 7001_ $$aPapageorgiou, A. C.
000097456 7001_ $$aTsoub, C.-C.
000097456 7001_ $$aWub, J.-J.
000097456 773__ $$0PERI:(DE-600)1461396-7$$a10.1016/j.bbrc.2010.06.071$$gVol. 398, p. 361-365$$p361-365$$q398<361-365$$tBiochemical and biophysical research communications$$v398$$x0006-291X$$y2010
000097456 85640 $$uhttp://www.ncbi.nlm.nih.gov/pubmed/20599728
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000097456 9141_ $$y2010
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000097456 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
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