001     97456
005     20250731113522.0
024 7 _ |a pmid:20599728
|2 pmid
024 7 _ |a 10.1016/j.bbrc.2010.06.071
|2 doi
024 7 _ |a 1090-2104
|2 ISSN
024 7 _ |a 0006-291X
|2 ISSN
024 7 _ |a WOS:000280867400005
|2 WOS
024 7 _ |a altmetric:123126834
|2 altmetric
024 7 _ |a openalex:W2090218121
|2 openalex
037 _ _ |a PHPPUBDB-20419
041 _ _ |a eng
082 _ _ |a 570
100 1 _ |a Haikarainen, T.
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a Structural characterization and biological implications of di-zinc binding in the ferroxidase center of Streptococcus pyogenes Dpr.
260 _ _ |a Orlando, Fla.
|b Academic Press
|c 2010
300 _ _ |a 361-365
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 Biochem. Biophys. Res. Commun.
|v 398
|y 3
|x 0006-291X
|0 PERI:(DE-600)1461396-7
500 _ _ |3 Converted on 2013-05-30 15:51
500 _ _ |3 Converted on 2013-06-21 19:21
520 _ _ |a 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.
536 _ _ |0 G:(DE-H253)POF2-K1.2-20130405
|f POF II
|x 0
|c POF2-54G13
|a DORIS Beamline K1.2 (POF2-54G13)
588 _ _ |a Dataset connected to Pubmed
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Bacterial Proteins: genetics
650 _ 2 |2 MeSH
|a Binding Sites
650 _ 2 |2 MeSH
|a Ceruloplasmin: chemistry
650 _ 2 |2 MeSH
|a Ceruloplasmin: genetics
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 Protein Conformation
650 _ 2 |2 MeSH
|a Streptococcus pyogenes: enzymology
650 _ 2 |2 MeSH
|a Zinc: chemistry
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 Dpr protein, Streptococcus
650 _ 7 |0 7440-66-6
|2 NLM Chemicals
|a Zinc
650 _ 7 |0 EC 1.16.3.1
|2 NLM Chemicals
|a Ceruloplasmin
693 _ _ |a DORIS III
|f DORIS Beamline K1.2
|1 EXP:(DE-H253)DORISIII-20150101
|0 EXP:(DE-H253)D-K1.2-20150101
|6 EXP:(DE-H253)D-K1.2-20150101
|x 0
700 1 _ |a Papageorgiou, A. C.
700 1 _ |a Tsoub, C.-C.
700 1 _ |a Wub, J.-J.
773 _ _ |0 PERI:(DE-600)1461396-7
|a 10.1016/j.bbrc.2010.06.071
|g Vol. 398, p. 361-365
|p 361-365
|q 398<361-365
|t Biochemical and biophysical research communications
|v 398
|x 0006-291X
|y 2010
856 4 0 |u http://www.ncbi.nlm.nih.gov/pubmed/20599728
909 C O |o oai:bib-pubdb1.desy.de:97456
|p VDB
910 1 _ |0 I:(DE-HGF)0
|a Externes Institut
|k Extern
913 1 _ |0 G:(DE-HGF)POF2-54G13
|1 G:(DE-HGF)POF2-540
|2 G:(DE-HGF)POF2-500
|9 G:(DE-H253)POF2-K1.2-20130405
|b Struktur der Materie
|v DORIS III
|x 0
|a DE-H253
|4 G:(DE-HGF)POF
|3 G:(DE-HGF)POF2
|l Forschung mit Photonen, Neutronen, Ionen
914 1 _ |y 2010
915 _ _ |a JCR/ISI refereed
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915 _ _ |a JCR
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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
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980 _ _ |a VDB
980 _ _ |a UNRESTRICTED
980 _ _ |a journal
980 _ _ |a I:(DE-H253)EMBL_-2012_-20130307
980 _ _ |a ConvertedRecord


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