Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori

Kurzanzeige
dc.contributor.authorFreigang, Jörgdeu
dc.contributor.authorDiederichs, Kay
dc.contributor.authorSchäfer, Klaus P.deu
dc.contributor.authorWelte, Wolfram
dc.contributor.authorPaul, Ralfdeu
dc.date.accessioned2011-03-24T17:43:46Zdeu
dc.date.available2011-03-24T17:43:46Zdeu
dc.date.issued2002deu
dc.description.abstractThe redox protein flavodoxin has been shown earlier to be reduced by the pyruvate-oxidoreductase (POR) enzyme complex of Helicobacter pylori, and also was proposed to be involved in the pathogenesis of gastric mucosa-associated lymphoid-tissue lymphoma (MALToma). Here, we report its X-ray structure, which is similar to flavodoxins of other bacteria and cyanobacteria. However, H. pylori flavodoxin has an alanine residue near the isoalloxazine ring of its cofactor flavin mononucleotide (FMN), while the other previously crystallized flavodoxins have a larger hydrophobic residue at this position. This creates a solute filled hole near the FMN cofactor of H. pylori flavodoxin. We also show that flavodoxin is essential for the survival of H. pylori, and conclude that its structure can be used as a starting point for the modeling of an inhibitor for the interaction between the POR-enzyme complex and flavodoxin.deu
dc.description.versionpublished
dc.format.mimetypeapplication/pdfdeu
dc.identifier.citationFirst publ. in: Protein Science 11 (2002), pp. 253 261deu
dc.identifier.doi10.1110/ps.28602
dc.identifier.pmid11790835
dc.identifier.ppn273985396deu
dc.identifier.urihttp://kops.uni-konstanz.de/handle/123456789/8450
dc.language.isoengdeu
dc.legacy.dateIssued2007deu
dc.rightsAttribution-NonCommercial-NoDerivs 2.0 Generic
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/2.0/
dc.subject.ddc570deu
dc.titleCrystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylorieng
dc.typeJOURNAL_ARTICLEdeu
dspace.entity.typePublication
kops.citation.bibtex
@article{Freigang2002Cryst-8450,
  year={2002},
  doi={10.1110/ps.28602},
  title={Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori},
  number={2},
  volume={11},
  issn={0961-8368},
  journal={Protein Science},
  pages={253--261},
  author={Freigang, Jörg and Diederichs, Kay and Schäfer, Klaus P. and Welte, Wolfram and Paul, Ralf}
}
kops.citation.iso690FREIGANG, Jörg, Kay DIEDERICHS, Klaus P. SCHÄFER, Wolfram WELTE, Ralf PAUL, 2002. Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori. In: Protein Science. 2002, 11(2), pp. 253-261. ISSN 0961-8368. eISSN 0961-8368. Available under: doi: 10.1110/ps.28602deu
kops.citation.iso690FREIGANG, Jörg, Kay DIEDERICHS, Klaus P. SCHÄFER, Wolfram WELTE, Ralf PAUL, 2002. Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori. In: Protein Science. 2002, 11(2), pp. 253-261. ISSN 0961-8368. eISSN 0961-8368. Available under: doi: 10.1110/ps.28602eng
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    <dcterms:abstract xml:lang="deu">The redox protein flavodoxin has been shown earlier to be reduced by the pyruvate-oxidoreductase (POR) enzyme complex of Helicobacter pylori, and also was proposed to be involved in the pathogenesis of gastric mucosa-associated lymphoid-tissue lymphoma (MALToma). Here, we report its X-ray structure, which is similar to flavodoxins of other bacteria and cyanobacteria. However, H. pylori flavodoxin has an alanine residue near the isoalloxazine ring of its cofactor flavin mononucleotide (FMN), while the other previously crystallized flavodoxins have a larger hydrophobic residue at this position. This creates a solute filled hole near the FMN cofactor of H. pylori flavodoxin. We also show that flavodoxin is essential for the survival of H. pylori, and conclude that its structure can be used as a starting point for the modeling of an inhibitor for the interaction between the POR-enzyme complex and flavodoxin.</dcterms:abstract>
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