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000085833 0247_ $$2pmid$$apmid:18552126
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000085833 0247_ $$2doi$$a10.1110/ps.036236.108
000085833 0247_ $$2ISSN$$a0961-8368
000085833 0247_ $$2ISSN$$a1469-896X
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000085833 037__ $$aPHPPUBDB-8588
000085833 041__ $$aeng
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000085833 1001_ $$aHavukainen, H.
000085833 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000085833 245__ $$aStructural basis of zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins
000085833 260__ $$aHoboken, NJ$$bWiley$$c2008
000085833 300__ $$a1513-1521
000085833 3367_ $$00$$2EndNote$$aJournal Article
000085833 3367_ $$2BibTeX$$aARTICLE
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000085833 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article$$mjournal
000085833 440_0 $$0PERI:(DE-600)2000025-X$$aProtein Sci.$$v17$$x0961-8368
000085833 500__ $$3Converted on 2013-05-30 12:33
000085833 500__ $$3Converted on 2013-06-21 19:20
000085833 520__ $$aStreptococcus suis Dpr is an iron-binding protein involved in oxidative stress resistance. It belongs to the bacterial Dps protein family whose members form dodecameric assemblies. Previous studies have shown that zinc and terbium inhibit iron incorporation in Listeria innocua Dps protein. In order to gain structural insights into the inhibitory effect of zinc and terbium, the crystal structures of Streptococcus suis Dpr complexes with these ions were determined at 1.8 A and 2.1 A, respectively. Both ions were found to bind at the ferroxidase center and in the same location as iron. In addition, a novel zinc-binding site formed by His40 and His44 was identified. Both His residues were found to be present within all known Streptococcus suis Dpr variants and in Streptococcus pneumoniae, Streptococcus gordonii, and Streptococcus sanguinis Dpr proteins. Amino acid sequence alignment of Dpr with other Dps family members revealed that His44 is highly conserved, in contrast to His40. The inhibitory effect of zinc and terbium on iron oxidation in Dpr was studied in vitro, and it was found that both ions at concentrations >0.2 mM almost completely abolish iron binding. These results provide a structural basis for the inhibitory effect of zinc and terbium in the Dps family of proteins, and suggest a potential role of the Dps proteins in zinc detoxification mechanisms involving the second zinc-binding site.
000085833 536__ $$0G:(DE-H253)POF1-No-Ref-20130405$$aFS Beamline without reference (POF1-550)$$cPOF1-550$$fPOF I$$x0
000085833 588__ $$aDataset connected to Pubmed
000085833 650_2 $$2MeSH$$aAmino Acid Sequence
000085833 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000085833 650_2 $$2MeSH$$aBacterial Proteins: genetics
000085833 650_2 $$2MeSH$$aBacterial Proteins: metabolism
000085833 650_2 $$2MeSH$$aBinding Sites
000085833 650_2 $$2MeSH$$aCeruloplasmin: antagonists & inhibitors
000085833 650_2 $$2MeSH$$aCrystallography, X-Ray
000085833 650_2 $$2MeSH$$aDNA-Binding Proteins: chemistry
000085833 650_2 $$2MeSH$$aDNA-Binding Proteins: genetics
000085833 650_2 $$2MeSH$$aDNA-Binding Proteins: metabolism
000085833 650_2 $$2MeSH$$aFerritins: metabolism
000085833 650_2 $$2MeSH$$aGenes, Bacterial
000085833 650_2 $$2MeSH$$aHistidine: chemistry
000085833 650_2 $$2MeSH$$aHumans
000085833 650_2 $$2MeSH$$aModels, Molecular
000085833 650_2 $$2MeSH$$aMolecular Sequence Data
000085833 650_2 $$2MeSH$$aProtein Binding
000085833 650_2 $$2MeSH$$aSequence Homology, Amino Acid
000085833 650_2 $$2MeSH$$aStreptococcus suis: chemistry
000085833 650_2 $$2MeSH$$aStreptococcus suis: genetics
000085833 650_2 $$2MeSH$$aStreptococcus suis: isolation & purification
000085833 650_2 $$2MeSH$$aStreptococcus suis: metabolism
000085833 650_2 $$2MeSH$$aTerbium: chemistry
000085833 650_2 $$2MeSH$$aTerbium: metabolism
000085833 650_2 $$2MeSH$$aWater: chemistry
000085833 650_2 $$2MeSH$$aZinc: chemistry
000085833 650_2 $$2MeSH$$aZinc: metabolism
000085833 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000085833 650_7 $$00$$2NLM Chemicals$$aDNA-Binding Proteins
000085833 650_7 $$00$$2NLM Chemicals$$aDPS protein, Bacteria
000085833 650_7 $$071-00-1$$2NLM Chemicals$$aHistidine
000085833 650_7 $$07440-27-9$$2NLM Chemicals$$aTerbium
000085833 650_7 $$07440-66-6$$2NLM Chemicals$$aZinc
000085833 650_7 $$07732-18-5$$2NLM Chemicals$$aWater
000085833 650_7 $$09007-73-2$$2NLM Chemicals$$aFerritins
000085833 650_7 $$0EC 1.16.3.1$$2NLM Chemicals$$aCeruloplasmin
000085833 693__ $$0EXP:(DE-H253)Unknown-BL-20150101$$6EXP:(DE-H253)Unknown-BL-20150101$$fUnknown DESY Beamline$$x0
000085833 7001_ $$aHaataja, S.
000085833 7001_ $$aKauko, A.
000085833 7001_ $$aPulliainen, A. T.
000085833 7001_ $$aSalminen, A.
000085833 7001_ $$aHaikarainen, T.
000085833 7001_ $$aFinne, J.
000085833 7001_ $$aPapageorgiou, A. C.
000085833 773__ $$0PERI:(DE-600)2000025-X$$a10.1110/ps.036236.108$$gVol. 17, p. 1513-1521$$p1513-1521$$q17<1513-1521$$tProtein science$$v17$$x0961-8368$$y2008
000085833 85640 $$uhttp://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&amp
000085833 85640 $$upubmedid=18552126
000085833 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC2525527
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000085833 9141_ $$a(c) 2008 The Protein Society. Free full text online!$$y2008
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000085833 920_1 $$iEuropean Molecular Biology Laboratory$$kEMBL
000085833 9201_ $$0I:(DE-H253)EMBL_-2012_-20130307$$kEMBL$$lEuropean Molecular Biology Laboratory$$x0
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