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

Abstract

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.

• Authors: Jörg Freigang, Kay Diederichs, Klaus P Schäfer, Wolfram Welte, Ralf Paul
• Journal: Protein science : a publication of the Protein Society (Protein Sci) Vol. 11 Issue 2 Pg. 253-61 (Feb 2002) ISSN: 0961-8368 [Print] United States
• PMID: 11790835 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• DNA Primers
• Flavodoxin
• Recombinant Proteins
• Flavin Mononucleotide

Topics

• Amino Acid Sequence
• Binding Sites
• Blotting, Southern
• Crystallization
• Crystallography, X-Ray
• DNA Primers (chemistry)
• Flavin Mononucleotide (chemistry)
• Flavodoxin (chemistry)
• Helicobacter pylori (chemistry)
• Hydrogen Bonding
• Magnetic Resonance Spectroscopy
• Models, Molecular
• Molecular Sequence Data
• Mutagenesis, Site-Directed
• Mutation (genetics)
• Polymerase Chain Reaction
• Protein Conformation
• Recombinant Proteins
• Sequence Homology, Amino Acid