View source for 4kpg


==Crystal structure of MycP1 from the ESX-1 type VII secretion system==
<StructureSection load='4kpg' size='340' side='right'caption='[[4kpg]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kpg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis_MC2_155 Mycolicibacterium smegmatis MC2 155]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KPG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KPG 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]] 2.148&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=4kpg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kpg OCA], [https://pdbe.org/4kpg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kpg RCSB], [https://www.ebi.ac.uk/pdbsum/4kpg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kpg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MYCP1_MYCS2 MYCP1_MYCS2] May play a dual role in regulation of ESX-1 secretion and virulence. Acts as a protease that cleaves EspB.<ref>PMID:20227664</ref> <ref>PMID:23620593</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mycobacteria use specialized type VII (ESX) secretion systems to export proteins across their complex cell walls. Mycobacterium tuberculosis encodes five nonredundant ESX secretion systems, with ESX-1 being particularly important to disease progression. All ESX loci encode extracellular membrane-bound proteases called mycosins (MycP) that are essential to secretion and have been shown to be involved in processing of type VII-exported proteins. Here, we report the first x-ray crystallographic structure of MycP1(24-407) to 1.86 A, defining a subtilisin-like fold with a unique N-terminal extension previously proposed to function as a propeptide for regulation of enzyme activity. The structure reveals that this N-terminal extension shows no structural similarity to previously characterized protease propeptides and instead wraps intimately around the catalytic domain where, tethered by a disulfide bond, it forms additional interactions with a unique extended loop that protrudes from the catalytic core. We also show MycP1 cleaves the ESX-1 secreted protein EspB from both M. tuberculosis and Mycobacterium smegmatis at a homologous cut site in vitro.

Structure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion System.,Solomonson M, Huesgen PF, Wasney GA, Watanabe N, Gruninger RJ, Prehna G, Overall CM, Strynadka NC J Biol Chem. 2013 Jun 14;288(24):17782-90. doi: 10.1074/jbc.M113.462036. Epub, 2013 Apr 25. PMID:23620593<ref>PMID:23620593</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kpg" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: Gruninger RJ]]
[[Category: Prehna G]]
[[Category: Solomonson M]]
[[Category: Strynadka NCJ]]
[[Category: Wasney GA]]
[[Category: Watanabe N]]