View source for 4lk4


==Structure of Vibrio cholerae VesB protease==
<StructureSection load='4lk4' size='340' side='right'caption='[[4lk4]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lk4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_569B Vibrio cholerae 569B]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LK4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LK4 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]] 2.4&#8491;</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=4lk4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lk4 OCA], [https://pdbe.org/4lk4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lk4 RCSB], [https://www.ebi.ac.uk/pdbsum/4lk4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lk4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9KSQ6_VIBCH Q9KSQ6_VIBCH] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The chymotrypsin subfamily A of serine proteases consists primarily of eukaryotic proteases, including only a few proteases of bacterial origin. VesB, a newly identified serine protease that is secreted by the type II secretion system in Vibrio cholerae, belongs to this subfamily. VesB is likely produced as a zymogen since sequence alignment with trypsinogen identified a putative cleavage site for activation and a catalytic triad, His-Asp-Ser. Using synthetic peptides, VesB efficiently cleaved a trypsin substrate, but not chymotrypsin and elastase substrates. The reversible serine protease inhibitor, benzamidine, inhibited VesB and served as an immobilized ligand for VesB affinity purification, further indicating its relationship with trypsin-like enzymes. Consistent with this family of serine proteases, N-terminal sequencing implied that the propeptide is removed in the secreted form of VesB. Separate mutagenesis of the activation site and catalytic serine rendered VesB inactive, confirming the importance of these features for activity, but not for secretion. Similar to trypsin but, in contrast to thrombin and other coagulation factors, Na+ did not stimulate the activity of VesB, despite containing the Tyr250 signature. The crystal structure of catalytically inactive pro-VesB revealed that the protease domain is structurally similar to trypsinogen. The C-terminal domain of VesB was found to adopt an immunoglobulin (Ig) fold that is structurally homologous to Ig folds of other extracellular Vibrio proteins. Possible roles of the Ig fold domain in stability, substrate specificity, cell surface association and type II secretion of VesB, the first bacterial multi-domain trypsin-like protease with known structure, are discussed.

Functional and structural characterization of Vibrio cholerae extracellular serine protease B, VesB.,Gadwal S, Korotkov KV, Delarosa JR, Hol WG, Sandkvist M J Biol Chem. 2014 Jan 23. PMID:24459146<ref>PMID:24459146</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lk4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vibrio cholerae 569B]]
[[Category: Delarosa JR]]
[[Category: Hol WGJ]]
[[Category: Korotkov KV]]