View source for 6aem


==Crystal structure of the PKD1 domain of Vibrio anguillarum Epp==
<StructureSection load='6aem' size='340' side='right'caption='[[6aem]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6aem]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_anguillarum Vibrio anguillarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AEM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AEM FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.272&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6aem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aem OCA], [https://pdbe.org/6aem PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6aem RCSB], [https://www.ebi.ac.uk/pdbsum/6aem PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6aem ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A383R4X5_VIBAN A0A383R4X5_VIBAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Extracellular proteases are often produced as pre-pro-enzyme and then undergo multiple processing steps to mature into the active form. The protease Epp, a virulent factor of Vibrio anguillarum, belongs to this family. Its maturation might be regulated by Ca(2+) via its polycystic kidney disease (PKD) domain, but the molecular mechanism is unknown. Herein, we report the crystal structure of the first PKD domain from V. anguillarum Epp (Epp-PKD1) and its specific Ca(2+)-binding capacity. Epp-PKD1 exists as a monomer, consisting of seven beta-strands which form two beta-sheets stacking with each other. One Ca(2+) is bound by the residues Asn3, Gln4, Asp27, Asp29, Asp68 and a water molecule with a pentagonal bipyramidal geometry. Incubating the apo Epp-PKD1 with Ca(2+) but not Mg(2+), Mn(2+), or Zn(2+), enhances the thermal and chemical stability of Epp-PKD1, indicating its specific binding to Ca(2+). Epp-PKD1 shares high similarity in both sequence and overall structure with that of Vibrio cholerae PrtV, a homologous protease of Epp, however, they differ in the oligomeric state and local structure at the Ca(2+)-binding site, suggesting maturation of PrtV and Epp might be differently regulated by Ca(2+). Likely, proteases may take advantage of the structural diversity in PKD domains to tune their Ca(2+)-regulated maturation process.

Structural basis for specific calcium binding by the polycystic-kidney-disease domain of Vibrio anguillarum protease Epp.,Li P, Zang K, Li Y, Liu C, Ma Q Biochem Biophys Res Commun. 2018 Oct 28;505(2):471-477. doi:, 10.1016/j.bbrc.2018.09.108. Epub 2018 Sep 27. PMID:30268503<ref>PMID:30268503</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6aem" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio anguillarum]]
[[Category: Li P]]
[[Category: Ma Q]]