1fue
From Proteopedia
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|PDB= 1fue |SIZE=350|CAPTION= <scene name='initialview01'>1fue</scene>, resolution 2.40Å | |PDB= 1fue |SIZE=350|CAPTION= <scene name='initialview01'>1fue</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FMN:FLAVIN MONONUCLEOTIDE'>FMN</scene> | + | |LIGAND= <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fue OCA], [http://www.ebi.ac.uk/pdbsum/1fue PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fue RCSB]</span> | ||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Schaefer, K P.]] | [[Category: Schaefer, K P.]] | ||
[[Category: Welte, W.]] | [[Category: Welte, W.]] | ||
| - | [[Category: FMN]] | ||
[[Category: flavoprotein]] | [[Category: flavoprotein]] | ||
[[Category: fmn]] | [[Category: fmn]] | ||
[[Category: helicobacter pylori]] | [[Category: helicobacter pylori]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:30:31 2008'' |
Revision as of 17:30, 30 March 2008
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| , resolution 2.40Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
FLAVODOXIN FROM HELICOBACTER PYLORI
Overview
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.
About this Structure
1FUE is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
Crystal structure of oxidized flavodoxin, an essential protein in Helicobacter pylori., Freigang J, Diederichs K, Schafer KP, Welte W, Paul R, Protein Sci. 2002 Feb;11(2):253-61. PMID:11790835
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