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2lu2
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==MIC5 regulates the activity of Toxoplasma subtilisin 1 by mimicking a subtilisin prodomain== | |
| + | <StructureSection load='2lu2' size='340' side='right'caption='[[2lu2]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2lu2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii Toxoplasma gondii]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LU2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LU2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lu2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lu2 OCA], [https://pdbe.org/2lu2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lu2 RCSB], [https://www.ebi.ac.uk/pdbsum/2lu2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lu2 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Toxoplasma gondii is the model parasite of the phylum Apicomplexa, which contains obligate intracellular parasites of medical and veterinary importance. Apicomplexans invade host cells by a multistep process involving the secretion of adhesive microneme protein (MIC) complexes. The subtilisin protease TgSUB1 trims several MICs on the parasite surface to activate gliding motility and host invasion. Although a previous study showed that expression of the secretory protein TgMIC5 suppresses TgSUB1 activity, the mechanism was unknown. Here, we solve the three-dimensional structure of TgMIC5 by nuclear magnetic resonance (NMR), revealing that it mimics a subtilisin prodomain including a flexible C-terminal peptide that may insert into the subtilisin active site. We show that TgMIC5 is an almost 50-fold more potent inhibitor of TgSUB1 activity than the small molecule inhibitor N-[N-(N-acetyl-l-leucyl)-l-leucyl]-l-norleucine (ALLN). Moreover, we demonstrate that TgMIC5 is retained on the parasite plasma membrane via its physical interaction with the membrane-anchored TgSUB1. | ||
| - | + | Microneme protein 5 regulates the activity of toxoplasma subtilisin 1 by mimicking a subtilisin prodomain.,Saouros S, Dou Z, Henry M, Marchant J, Carruthers VB, Matthews S J Biol Chem. 2012 Oct 19;287(43):36029-40. doi: 10.1074/jbc.M112.389825. Epub, 2012 Aug 15. PMID:22896704<ref>PMID:22896704</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2lu2" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Toxoplasma gondii]] | ||
| + | [[Category: Carruthers VB]] | ||
| + | [[Category: Dou Z]] | ||
| + | [[Category: Henry M]] | ||
| + | [[Category: Marchant J]] | ||
| + | [[Category: Matthews S]] | ||
| + | [[Category: Saouros S]] | ||
Current revision
MIC5 regulates the activity of Toxoplasma subtilisin 1 by mimicking a subtilisin prodomain
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