1fue

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(New page: 200px<br /><applet load="1fue" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fue, resolution 2.40&Aring;" /> '''FLAVODOXIN FROM HELI...)
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[[Image:1fue.gif|left|200px]]<br /><applet load="1fue" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fue.gif|left|200px]]<br /><applet load="1fue" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fue, resolution 2.40&Aring;" />
caption="1fue, resolution 2.40&Aring;" />
'''FLAVODOXIN FROM HELICOBACTER PYLORI'''<br />
'''FLAVODOXIN FROM HELICOBACTER PYLORI'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1FUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with FMN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FUE OCA].
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1FUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori] with <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUE OCA].
==Reference==
==Reference==
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[[Category: Freigang, J.]]
[[Category: Freigang, J.]]
[[Category: Paul, R.]]
[[Category: Paul, R.]]
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[[Category: Schaefer, K.P.]]
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[[Category: Schaefer, K P.]]
[[Category: Welte, W.]]
[[Category: Welte, W.]]
[[Category: FMN]]
[[Category: FMN]]
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[[Category: helicobacter pylori]]
[[Category: helicobacter pylori]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:17:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:42:43 2008''

Revision as of 10:42, 21 February 2008


1fue, resolution 2.40Å

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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 with as ligand. 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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