View source for 4kb5


==Crystal structure of MycP1 from Mycobacterium smegmatis==
<StructureSection load='4kb5' size='340' side='right'caption='[[4kb5]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4kb5]] 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=4KB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4KB5 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4kb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4kb5 OCA], [https://pdbe.org/4kb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4kb5 RCSB], [https://www.ebi.ac.uk/pdbsum/4kb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4kb5 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 ==
Mycosin-1 protease (MycP1) is a serine protease anchored to the inner membrane of Mycobacterium tuberculosis, and is essential in virulence factor secretion through the ESX-1 type VII secretion system (T7SS). Bacterial physiology studies demonstrated that MycP1 plays a dual role in the regulation of ESX-1 secretion and virulence, primarily through cleavage of its secretion substrate EspB. MycP1 contains a putative N-terminal inhibitory propeptide and a catalytic triad of Asp-His-Ser, classic hallmarks of a subtilase family serine protease. The MycP1 propeptide was previously reported to be initially inactive and activated after prolonged incubation. In this study, we have determined crystal structures of MycP1 with (MycP1(2)(4)(-)(4)(2)(2)) and without (MycP1(6)(3)(-)(4)(2)(2)) the propeptide, and conducted EspB cleavage assays using the two proteins. Very high structural similarity was observed in the two crystal structures. Interestingly, protease assays demonstrated positive EspB cleavage for both proteins, indicating that the putative propeptide does not inhibit protease activity. Molecular dynamic simulations showed higher rigidity in regions guarding the entrance to the catalytic site in MycP1(2)(4)(-)(4)(2)(2) than in MycP1(6)(3)(-)(4)(2)(2), suggesting that the putative propeptide might contribute to the conformational stability of the active site cleft and surrounding regions.

The putative propeptide of MycP1 in mycobacterial type VII secretion system does not inhibit protease activity but improves protein stability.,Sun D, Liu Q, He Y, Wang C, Wu F, Tian C, Zang J Protein Cell. 2013 Dec;4(12):921-31. doi: 10.1007/s13238-013-3089-7. Epub 2013, Nov 18. PMID:24248472<ref>PMID:24248472</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4kb5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium smegmatis MC2 155]]
[[Category: He Y]]
[[Category: Sun DM]]
[[Category: Tian CL]]