7pty: Difference between revisions
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New page: '''Unreleased structure''' The entry 7pty is ON HOLD Authors: Chen, M., Gatsogiannis, C. Description: Alpha-latrocrustotoxin monomer Category: Unreleased Structures [[Category: Che... |
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The | ==Delta-latroinsectotoxin dimer== | ||
<StructureSection load='7pty' size='340' side='right'caption='[[7pty]], [[Resolution|resolution]] 4.63Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PTY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PTY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.63Å</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=7pty FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pty OCA], [https://pdbe.org/7pty PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pty RCSB], [https://www.ebi.ac.uk/pdbsum/7pty PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pty ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Latrotoxins (LaTXs) are presynaptic pore-forming neurotoxins found in the venom of Latrodectus spiders. The venom contains a toxic cocktail of seven LaTXs, with one of them targeting vertebrates (alpha-latrotoxin (alpha-LTX)), five specialized on insects (alpha, beta, gamma, delta, epsilon- latroinsectotoxins (LITs), and one on crustaceans (alpha-latrocrustatoxin (alpha-LCT)). LaTXs bind to specific receptors on the surface of neuronal cells, inducing the release of neurotransmitters either by directly stimulating exocytosis or by forming Ca(2+)-conductive tetrameric pores in the membrane. Despite extensive studies in the past decades, a high-resolution structure of a LaTX is not yet available and the precise mechanism of LaTX action remains unclear. Here, we report cryoEM structures of the alpha-LCT monomer and the delta-LIT dimer. The structures reveal that LaTXs are organized in four domains. A C-terminal domain of ankyrin-like repeats shields a central membrane insertion domain of six parallel alpha-helices. Both domains are flexibly linked via an N-terminal alpha-helical domain and a small beta-sheet domain. A comparison between the structures suggests that oligomerization involves major conformational changes in LaTXs with longer C-terminal domains. Based on our data we propose a cyclic mechanism of oligomerization, taking place prior membrane insertion. Both recombinant alpha-LCT and delta-LIT form channels in artificial membrane bilayers, that are stabilized by Ca(2+) ions and allow calcium flux at negative membrane potentials. Our comparative analysis between alpha-LCT and delta-LIT provides first crucial insights towards understanding the molecular mechanism of the LaTX family. | |||
Molecular architecture of black widow spider neurotoxins.,Chen M, Blum D, Engelhard L, Raunser S, Wagner R, Gatsogiannis C Nat Commun. 2021 Nov 29;12(1):6956. doi: 10.1038/s41467-021-26562-8. PMID:34845192<ref>PMID:34845192</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Chen | <div class="pdbe-citations 7pty" style="background-color:#fffaf0;"></div> | ||
[[Category: Gatsogiannis | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Chen M]] | |||
[[Category: Gatsogiannis C]] | |||
