1FUE
FLAVODOXIN FROM HELICOBACTER PYLORI
Summary for 1FUE
| Entry DOI | 10.2210/pdb1fue/pdb |
| Descriptor | FLAVODOXIN, FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | flavoprotein, helicobacter pylori, fmn, electron transport |
| Biological source | Helicobacter pylori |
| Total number of polymer chains | 1 |
| Total formula weight | 17761.41 |
| Authors | Freigang, J.,Diederichs, K.,Schaefer, K.P.,Welte, W.,Paul, R. (deposition date: 2000-09-15, release date: 2002-02-06, Last modification date: 2024-02-07) |
| Primary citation | Freigang, J.,Diederichs, K.,Schafer, K.P.,Welte, W.,Paul, R. Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori. Protein Sci., 11:253-261, 2002 Cited by PubMed 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. PubMed: 11790835DOI: 10.1110/ps.28602 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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