3u34

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Current revision (13:47, 14 March 2024) (edit) (undo)
 
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<StructureSection load='3u34' size='340' side='right'caption='[[3u34]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='3u34' size='340' side='right'caption='[[3u34]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3u34]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U34 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3u34]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_citri Xanthomonas citri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U34 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3dmb|3dmb]], [[1flm|1flm]], [[2ou5|2ou5]], [[2i02|2i02]], [[3u35|3u35]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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=3u34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u34 OCA], [https://pdbe.org/3u34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u34 RCSB], [https://www.ebi.ac.uk/pdbsum/3u34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u34 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=3u34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u34 OCA], [https://pdbe.org/3u34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u34 RCSB], [https://www.ebi.ac.uk/pdbsum/3u34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u34 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q8PK08_XANAC Q8PK08_XANAC]
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Xanthomonas citri pv. citri (Xac) causes citrus canker and affects citrus agriculture worldwide. Functional genetic analysis has indicated that a putative general stress protein (XacGSP) encoded by the Xac2369 gene is involved in the bacterial infection. In this report, the crystal structure of XacGSP was determined to 2.5 A resolution. There are four XacGSP molecules in the crystal asymmetric unit. Each XacGSP monomer folds into a six-stranded antiparallel beta-barrel flanked by five alpha-helices. A C-terminal extension protrudes from the sixth beta-strand of the beta-barrel and pairs with its counterpart from another monomer to form a bridge between the two subunits of an XacGSP dimer. Two XacGSP dimers cross over each other to form a tetramer; the beta-barrels from one dimer contact the beta-barrels of the other, while the two bridges are distant from each other and do not make contacts. The three-dimensional structure of the XacGSP monomer is very similar to those of pyridoxine 5-phosphate oxidases, a group of enzymes that use flavin mononucleotide (FMN) as a cofactor. Consistent with this, purified XacGSP protein binds to both FMN and flavin adenine dinucleotide (FAD), suggesting that XacGSP may help the bacteria to react against the oxidative stress induced by the defense mechanisms of the plant.
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The structure of a Xanthomonas general stress protein involved in citrus canker reveals its flavin-binding property.,Hilario E, Li Y, Niks D, Fan L Acta Crystallogr D Biol Crystallogr. 2012 Jul;68(Pt 7):846-53. doi:, 10.1107/S0907444912014126. Epub 2012 Jun 19. PMID:22751670<ref>PMID:22751670</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3u34" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fan, L]]
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[[Category: Xanthomonas citri]]
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[[Category: Hilario, E]]
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[[Category: Fan L]]
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[[Category: Li, Y]]
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[[Category: Hilario E]]
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[[Category: Fmn fad]]
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[[Category: Li Y]]
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[[Category: Pnp-oxidase like fold]]
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[[Category: Protein binding]]
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[[Category: Xanthomonas citri general stress protein fmn binding protein fad binding protein]]
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Current revision

Crystal structure of the general stress FMN/FAD binding protein from the phytopathogen Xanthomonas citri

PDB ID 3u34

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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