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| | ==Crystal structure of MycP1 from the ESX-1 type VII secretion system== | | ==Crystal structure of MycP1 from the ESX-1 type VII secretion system== |
| - | <StructureSection load='4j94' size='340' side='right' caption='[[4j94]], [[Resolution|resolution]] 1.86Å' scene=''> | + | <StructureSection load='4j94' size='340' side='right'caption='[[4j94]], [[Resolution|resolution]] 1.86Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j94]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mycs2 Mycs2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J94 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J94 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j94]] 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=4J94 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J94 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSMEG_0083, MSMEI_0081 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246196 MYCS2])</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=4j94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j94 OCA], [https://pdbe.org/4j94 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j94 RCSB], [https://www.ebi.ac.uk/pdbsum/4j94 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j94 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] </span></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=4j94 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j94 OCA], [http://pdbe.org/4j94 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j94 RCSB], [http://www.ebi.ac.uk/pdbsum/4j94 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j94 ProSAT]</span></td></tr> | + | |
| | </table> | | </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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Mycs2]] | + | [[Category: Large Structures]] |
| - | [[Category: Subtilisin]] | + | [[Category: Mycolicibacterium smegmatis MC2 155]] |
| - | [[Category: Gruninger, R J]] | + | [[Category: Gruninger RJ]] |
| - | [[Category: Prehna, G]] | + | [[Category: Prehna G]] |
| - | [[Category: Solomonson, M]] | + | [[Category: Solomonson M]] |
| - | [[Category: Strynadka, N C.J]] | + | [[Category: Strynadka NCJ]] |
| - | [[Category: Wasney, G A]] | + | [[Category: Wasney GA]] |
| - | [[Category: Watanabe, N]] | + | [[Category: Watanabe N]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Protease]]
| + | |
| - | [[Category: Secretion system]]
| + | |
| - | [[Category: Subtilisin-like]]
| + | |
| Structural highlights
Function
MYCP1_MYCS2 May play a dual role in regulation of ESX-1 secretion and virulence. Acts as a protease that cleaves EspB.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ohol YM, Goetz DH, Chan K, Shiloh MU, Craik CS, Cox JS. Mycobacterium tuberculosis MycP1 protease plays a dual role in regulation of ESX-1 secretion and virulence. Cell Host Microbe. 2010 Mar 18;7(3):210-20. doi: 10.1016/j.chom.2010.02.006. PMID:20227664 doi:http://dx.doi.org/10.1016/j.chom.2010.02.006
- ↑ Solomonson M, Huesgen PF, Wasney GA, Watanabe N, Gruninger RJ, Prehna G, Overall CM, Strynadka NC. Structure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion System. J Biol Chem. 2013 Jun 14;288(24):17782-90. doi: 10.1074/jbc.M113.462036. Epub, 2013 Apr 25. PMID:23620593 doi:10.1074/jbc.M113.462036
- ↑ Solomonson M, Huesgen PF, Wasney GA, Watanabe N, Gruninger RJ, Prehna G, Overall CM, Strynadka NC. Structure of the Mycosin-1 Protease from the Mycobacterial ESX-1 Protein Type VII Secretion System. J Biol Chem. 2013 Jun 14;288(24):17782-90. doi: 10.1074/jbc.M113.462036. Epub, 2013 Apr 25. PMID:23620593 doi:10.1074/jbc.M113.462036
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