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<StructureSection load='1fue' size='340' side='right'caption='[[1fue]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1fue' size='340' side='right'caption='[[1fue]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1fue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUE FirstGlance]. <br>
<table><tr><td colspan='2'>[[1fue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FUE FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fue OCA], [https://pdbe.org/1fue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fue RCSB], [https://www.ebi.ac.uk/pdbsum/1fue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fue ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fue OCA], [https://pdbe.org/1fue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fue RCSB], [https://www.ebi.ac.uk/pdbsum/1fue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fue ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FLAV_HELPJ FLAV_HELPJ]] Low-potential electron donor to a number of redox enzymes (By similarity).  
[https://www.uniprot.org/uniprot/FLAV_HELPJ FLAV_HELPJ] Low-potential electron donor to a number of redox enzymes (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fue ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fue ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:11790835</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fue" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
*[[Flavodoxin 3D structures|Flavodoxin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43504]]
[[Category: Helicobacter pylori]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Diederichs, K]]
[[Category: Diederichs K]]
[[Category: Freigang, J]]
[[Category: Freigang J]]
[[Category: Paul, R]]
[[Category: Paul R]]
[[Category: Schaefer, K P]]
[[Category: Schaefer KP]]
[[Category: Welte, W]]
[[Category: Welte W]]
[[Category: Electron transport]]
[[Category: Flavoprotein]]
[[Category: Fmn]]
[[Category: Helicobacter pylori]]

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