% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Havukainen:85833,
      author       = {Havukainen, H. and Haataja, S. and Kauko, A. and
                      Pulliainen, A. T. and Salminen, A. and Haikarainen, T. and
                      Finne, J. and Papageorgiou, A. C. and DESY},
      title        = {{S}tructural basis of zinc- and terbium-mediated inhibition
                      of ferroxidase activity in {D}ps ferritin-like proteins},
      journal      = {Protein science},
      volume       = {17},
      issn         = {0961-8368},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {PHPPUBDB-8588},
      pages        = {1513-1521},
      year         = {2008},
      abstract     = {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.},
      keywords     = {Amino Acid Sequence / Bacterial Proteins: chemistry /
                      Bacterial Proteins: genetics / Bacterial Proteins:
                      metabolism / Binding Sites / Ceruloplasmin: antagonists $\&$
                      inhibitors / Crystallography, X-Ray / DNA-Binding Proteins:
                      chemistry / DNA-Binding Proteins: genetics / DNA-Binding
                      Proteins: metabolism / Ferritins: metabolism / Genes,
                      Bacterial / Histidine: chemistry / Humans / Models,
                      Molecular / Molecular Sequence Data / Protein Binding /
                      Sequence Homology, Amino Acid / Streptococcus suis:
                      chemistry / Streptococcus suis: genetics / Streptococcus
                      suis: isolation $\&$ purification / Streptococcus suis:
                      metabolism / Terbium: chemistry / Terbium: metabolism /
                      Water: chemistry / Zinc: chemistry / Zinc: metabolism /
                      Bacterial Proteins (NLM Chemicals) / DNA-Binding Proteins
                      (NLM Chemicals) / DPS protein, Bacteria (NLM Chemicals) /
                      Histidine (NLM Chemicals) / Terbium (NLM Chemicals) / Zinc
                      (NLM Chemicals) / Water (NLM Chemicals) / Ferritins (NLM
                      Chemicals) / Ceruloplasmin (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {610},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:18552126},
      pmc          = {pmc:PMC2525527},
      UT           = {WOS:000258651900006},
      doi          = {10.1110/ps.036236.108},
      url          = {https://bib-pubdb1.desy.de/record/85833},
}