| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Fachbereich Biologie, Universität Konstanz, D-78457 Konstanz, Germany
2 Byk Gulden Pharmaceuticals, Department of Molecular Biology, D-78403 Konstanz, Germany
3 Division of Molecular Microbiology, Biozentrum, University of Basel, 4056 Basel, Switzerland
Reprint requests to: Ralf Paul, Division of Molecular Microbiology, Biozentrum, University of Basel, Klingelbergstrasse 50/70, 4056 Basel, Switzerland.
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.
CiteULike 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  N. Cremades and J. Sancho Molten Globule and Native State Ensemble of Helicobacter pylori Flavodoxin: Can Crowding, Osmolytes or Cofactors Stabilize the Native Conformation Relative to the Molten Globule? Biophys. J., August 15, 2008; 95(4): 1913 - 1927. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. R. Weerakoon and J. W. Olson The Campylobacter jejuni NADH:Ubiquinone Oxidoreductase (Complex I) Utilizes Flavodoxin Rather than NADH J. Bacteriol., February 1, 2008; 190(3): 915 - 925. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 N. Cremades, M. Bueno, J. L. Neira, A. Velazquez-Campoy, and J. Sancho Conformational Stability of Helicobacter pylori Flavodoxin: FIT TO FUNCTION AT pH 5 J. Biol. Chem., February 1, 2008; 283(5): 2883 - 2895. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
H. Shimomura, S. Hayashi, K. Yokota, K. Oguma, and Y. Hirai Conversion of Flavodoxin from Holoenzyme to Apoprotein during Growth Phase Changes in Helicobacter pylori J. Bacteriol., July 1, 2007; 189(13): 4960 - 4963. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Y. Hu, Y. Li, X. Zhang, X. Guo, B. Xia, and C. Jin Solution Structures and Backbone Dynamics of a Flavodoxin MioC from Escherichia coli in both Apo- and Holo-forms: IMPLICATIONS FOR COFACTOR BINDING AND ELECTRON TRANSFER J. Biol. Chem., November 17, 2006; 281(46): 35454 - 35466. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Alagaratnam, G. van Pouderoyen, T. Pijning, B. W. Dijkstra, D. Cavazzini, G. L. Rossi, W. M.A.M. Van Dongen, C. P.M. van Mierlo, W. J. H. van Berkel, and G. W. Canters A crystallographic study of Cys69Ala flavodoxin II from Azotobacter vinelandii: Structural determinants of redox potential Protein Sci., September 1, 2005; 14(9): 2284 - 2295. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. L. A. Andrade, F. Cruz, C. L. Drennan, V. Ramakrishnan, D. C. Rees, J. G. Ferry, and O. Einsle Structures of the Iron-Sulfur Flavoproteins from Methanosarcina thermophila and Archaeoglobus fulgidus J. Bacteriol., June 1, 2005; 187(11): 3848 - 3854. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
R. Neeli, O. Roitel, N. S. Scrutton, and A. W. Munro Switching Pyridine Nucleotide Specificity in P450 BM3: MECHANISTIC ANALYSIS OF THE W1046H AND W1046A ENZYMES J. Biol. Chem., May 6, 2005; 280(18): 17634 - 17644. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. Liger, M. Graille, C.-Z. Zhou, N. Leulliot, S. Quevillon-Cheruel, K. Blondeau, J. Janin, and H. van Tilbeurgh Crystal Structure and Functional Characterization of Yeast YLR011wp, an Enzyme with NAD(P)H-FMN and Ferric Iron Reductase Activities J. Biol. Chem., August 13, 2004; 279(33): 34890 - 34897. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Lostao, F. Daoudi, M. P. Irun, A. Ramon, C. Fernandez-Cabrera, A. Romero, and J. Sancho How FMN Binds to Anabaena Apoflavodoxin: A HYDROPHOBIC ENCOUNTER AT AN OPEN BINDING SITE J. Biol. Chem., June 20, 2003; 278(26): 24053 - 24061. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
