6hox
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of the binding domain of Paraclostridial Mosquitocidal Protein 1== | |
| + | <StructureSection load='6hox' size='340' side='right'caption='[[6hox]], [[Resolution|resolution]] 1.95Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6hox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraclostridium_bifermentans Paraclostridium bifermentans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HOX 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]] 1.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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=6hox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hox OCA], [https://pdbe.org/6hox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hox RCSB], [https://www.ebi.ac.uk/pdbsum/6hox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hox ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A5P3XKQ1_PARBF A0A5P3XKQ1_PARBF] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Clostridial neurotoxins, including tetanus and botulinum neurotoxins, generally target vertebrates. We show here that this family of toxins has a much broader host spectrum, by identifying PMP1, a clostridial-like neurotoxin that selectively targets anopheline mosquitoes. Isolation of PMP1 from Paraclostridium bifermentans strains collected in anopheline endemic areas on two continents indicates it is widely distributed. The toxin likely evolved from an ancestral form that targets the nervous system of similar organisms, using a common mechanism that disrupts SNARE-mediated exocytosis. It cleaves the mosquito syntaxin and employs a unique receptor recognition strategy. Our research has an important impact on the study of the evolution of clostridial neurotoxins and provides the basis for the use of P. bifermentans strains and PMP1 as innovative, environmentally friendly approaches to reduce malaria through anopheline control. | ||
| - | + | A neurotoxin that specifically targets Anopheles mosquitoes.,Contreras E, Masuyer G, Qureshi N, Chawla S, Dhillon HS, Lee HL, Chen J, Stenmark P, Gill SS Nat Commun. 2019 Jun 28;10(1):2869. doi: 10.1038/s41467-019-10732-w. PMID:31253776<ref>PMID:31253776</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6hox" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Paraclostridium bifermentans]] | ||
| + | [[Category: Masuyer G]] | ||
| + | [[Category: Stenmark P]] | ||
Current revision
Crystal structure of the binding domain of Paraclostridial Mosquitocidal Protein 1
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