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3rqa

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Current revision (08:36, 20 March 2024) (edit) (undo)
 
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<StructureSection load='3rqa' size='340' side='right'caption='[[3rqa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3rqa' size='340' side='right'caption='[[3rqa]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3rqa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xancb Xancb]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RQA FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3rqa]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._campestris_str._B100 Xanthomonas campestris pv. campestris str. B100]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RQA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RQA 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=ACT:ACETATE+ION'>ACT</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]] 2.1&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">xcc-b100_2234 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=509169 XANCB])</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=ACT:ACETATE+ION'>ACT</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=3rqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rqa OCA], [https://pdbe.org/3rqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rqa RCSB], [https://www.ebi.ac.uk/pdbsum/3rqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rqa 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=3rqa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rqa OCA], [https://pdbe.org/3rqa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rqa RCSB], [https://www.ebi.ac.uk/pdbsum/3rqa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rqa 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/B0RT03_XANCB B0RT03_XANCB]
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PilZ domain is one of the key receptors for the newly discovered secondary messenger molecule cyclic di-GMP (c-di-GMP). To date, several monomeric PilZ domain proteins have been identified. Some exhibit strong c-di-GMP binding activity, while others have barely detectable c-di-GMP binding activity and require an accessory protein such as FimX to indirectly respond to the c-di-GMP signal. We now report a novel tetrameric PilZ domain structure of XCC6012 from the plant pathogen Xanthomonas campestris pv. campestris (Xcc). It is one of the four PilZ domain proteins essential for Xcc pathogenicity. Although the monomer adopts a structure similar to those of the PilZ domains with very weak c-di-GMP binding activity, it is nevertheless interrupted in the middle by two extra long helices. Four XCC6012 proteins are thus self-assembled into a tetramer via the extra heptad repeat alpha3 helices to form a parallel four-stranded coiled-coil, which is further enclosed by two sets of inclined alpha2 and alpha4 helices. We further generated a series of XCC6012 variants and measured the unfolding temperatures and oligomeric states in order to investigate the nature of this novel tetramer. Discovery of this new PilZ domain architecture increases the complexity of c-di-GMP-mediated regulation.
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A novel tetrameric PilZ domain structure from xanthomonads.,Li TN, Chin KH, Fung KM, Yang MT, Wang AH, Chou SH PLoS One. 2011;6(7):e22036. Epub 2011 Jul 7. PMID:21760949<ref>PMID:21760949</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 3rqa" 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: Xancb]]
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[[Category: Xanthomonas campestris pv. campestris str. B100]]
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[[Category: Chin, K H]]
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[[Category: Chin K-H]]
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[[Category: Chou, S H]]
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[[Category: Chou S-H]]
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[[Category: Li, T N]]
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[[Category: Li T-N]]
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[[Category: Four helix bundle]]
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[[Category: Pilz domain]]
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[[Category: Tetrameric parallel coiled-coil]]
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[[Category: Unknown function]]
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Current revision

The Crystal Structure of a Pathogenic Protein from the Xanthomonas campestris Reveals a New Tetrameric PilZ Domain Self-Assembled via a Unusual Helical Bundle

PDB ID 3rqa

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