6aem: Difference between revisions
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The | ==Crystal structure of the PKD1 domain of Vibrio anguillarum Epp== | ||
<StructureSection load='6aem' size='340' side='right' caption='[[6aem]], [[Resolution|resolution]] 1.27Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6aem]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AEM FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6aem FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6aem OCA], [http://pdbe.org/6aem PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6aem RCSB], [http://www.ebi.ac.uk/pdbsum/6aem PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6aem ProSAT]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6aem" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Li, P]] | |||
[[Category: Ma, Q]] | [[Category: Ma, Q]] | ||
[[Category: | [[Category: Polycystic kidney disease domain]] | ||
[[Category: Protease]] | |||
[[Category: Unknown function]] | |||
