1fue: Difference between revisions
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<StructureSection load='1fue' size='340' side='right'caption='[[1fue]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1fue' size='340' side='right'caption='[[1fue]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1fue]] is a 1 chain structure with sequence from [ | <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> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | </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'>[ | <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). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:12, 13 October 2021
FLAVODOXIN FROM HELICOBACTER PYLORIFLAVODOXIN FROM HELICOBACTER PYLORI
Structural highlights
Function[FLAV_HELPJ] Low-potential electron donor to a number of redox enzymes (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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