001     85833
005     20250731122906.0
024 7 _ |a pmid:18552126
|2 pmid
024 7 _ |a pmc:PMC2525527
|2 pmc
024 7 _ |a 10.1110/ps.036236.108
|2 doi
024 7 _ |a 0961-8368
|2 ISSN
024 7 _ |a 1469-896X
|2 ISSN
024 7 _ |a WOS:000258651900006
|2 WOS
024 7 _ |a altmetric:24185514
|2 altmetric
024 7 _ |a openalex:W1996409611
|2 openalex
037 _ _ |a PHPPUBDB-8588
041 _ _ |a eng
082 _ _ |a 610
100 1 _ |a Havukainen, H.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a Structural basis of zinc- and terbium-mediated inhibition of ferroxidase activity in Dps ferritin-like proteins
260 _ _ |a Hoboken, NJ
|b Wiley
|c 2008
300 _ _ |a 1513-1521
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a article
|2 DRIVER
336 7 _ |a Journal Article
|m journal
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
440 _ 0 |a Protein Sci.
|v 17
|x 0961-8368
|0 PERI:(DE-600)2000025-X
500 _ _ |3 Converted on 2013-05-30 12:33
500 _ _ |3 Converted on 2013-06-21 19:20
520 _ _ |a Streptococcus 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.
536 _ _ |0 G:(DE-H253)POF1-No-Ref-20130405
|f POF I
|x 0
|c POF1-550
|a FS Beamline without reference (POF1-550)
588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Amino Acid Sequence
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Bacterial Proteins: genetics
650 _ 2 |2 MeSH
|a Bacterial Proteins: metabolism
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Ceruloplasmin: antagonists & inhibitors
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a DNA-Binding Proteins: chemistry
650 _ 2 |2 MeSH
|a DNA-Binding Proteins: genetics
650 _ 2 |2 MeSH
|a DNA-Binding Proteins: metabolism
650 _ 2 |2 MeSH
|a Ferritins: metabolism
650 _ 2 |2 MeSH
|a Genes, Bacterial
650 _ 2 |2 MeSH
|a Histidine: chemistry
650 _ 2 |2 MeSH
|a Humans
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Sequence Data
650 _ 2 |2 MeSH
|a Protein Binding
650 _ 2 |2 MeSH
|a Sequence Homology, Amino Acid
650 _ 2 |2 MeSH
|a Streptococcus suis: chemistry
650 _ 2 |2 MeSH
|a Streptococcus suis: genetics
650 _ 2 |2 MeSH
|a Streptococcus suis: isolation & purification
650 _ 2 |2 MeSH
|a Streptococcus suis: metabolism
650 _ 2 |2 MeSH
|a Terbium: chemistry
650 _ 2 |2 MeSH
|a Terbium: metabolism
650 _ 2 |2 MeSH
|a Water: chemistry
650 _ 2 |2 MeSH
|a Zinc: chemistry
650 _ 2 |2 MeSH
|a Zinc: metabolism
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a DNA-Binding Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a DPS protein, Bacteria
650 _ 7 |0 71-00-1
|2 NLM Chemicals
|a Histidine
650 _ 7 |0 7440-27-9
|2 NLM Chemicals
|a Terbium
650 _ 7 |0 7440-66-6
|2 NLM Chemicals
|a Zinc
650 _ 7 |0 7732-18-5
|2 NLM Chemicals
|a Water
650 _ 7 |0 9007-73-2
|2 NLM Chemicals
|a Ferritins
650 _ 7 |0 EC 1.16.3.1
|2 NLM Chemicals
|a Ceruloplasmin
693 _ _ |0 EXP:(DE-H253)Unknown-BL-20150101
|f Unknown DESY Beamline
|x 0
|6 EXP:(DE-H253)Unknown-BL-20150101
700 1 _ |a Haataja, S.
700 1 _ |a Kauko, A.
700 1 _ |a Pulliainen, A. T.
700 1 _ |a Salminen, A.
700 1 _ |a Haikarainen, T.
700 1 _ |a Finne, J.
700 1 _ |a Papageorgiou, A. C.
773 _ _ |0 PERI:(DE-600)2000025-X
|a 10.1110/ps.036236.108
|g Vol. 17, p. 1513-1521
|p 1513-1521
|q 17<1513-1521
|t Protein science
|v 17
|x 0961-8368
|y 2008
856 4 0 |u http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pubmed&
856 4 0 |u pubmedid=18552126
856 7 _ |2 Pubmed Central
|u http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2525527
909 C O |o oai:bib-pubdb1.desy.de:85833
|p VDB
910 1 _ |0 I:(DE-HGF)0
|a Externes Institut
|k Extern
913 1 _ |0 G:(DE-HGF)POF1-540
|9 G:(DE-H253)POF1-No-Ref-20130405
|v Kondensierte Materie
|x 0
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|4 G:(DE-HGF)POF
|1 G:(DE-HGF)POF1-550
|3 G:(DE-HGF)POF1
|2 G:(DE-HGF)POF1-500
|b Struktur der Materie
|l Großgeräte für die Forschung mit Photonen, Neutronen, Ionen
914 1 _ |a (c) 2008 The Protein Society. Free full text online!
|y 2008
915 _ _ |a JCR/ISI refereed
|0 StatID:(DE-HGF)0010
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915 _ _ |a JCR
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915 _ _ |a DBCoverage
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915 _ _ |a No Author Disambiguation
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920 _ 1 |k EMBL
|i European Molecular Biology Laboratory
920 1 _ |0 I:(DE-H253)EMBL_-2012_-20130307
|k EMBL
|l European Molecular Biology Laboratory
|x 0
920 _ _ |k 001
980 _ _ |a PHPPUBDB
980 _ _ |a VDB
980 _ _ |a UNRESTRICTED
980 _ _ |a journal
980 _ _ |a I:(DE-H253)EMBL_-2012_-20130307
980 _ _ |a ConvertedRecord


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