8sl0: Difference between revisions
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New page: '''Unreleased structure''' The entry 8sl0 is ON HOLD Authors: Johnson, A.G., Mayer, M.L., Kranzusch, P.J. Description: Structure of a bacterial gasdermin slinky-like oligomer [[Categor... |
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==Structure of a bacterial gasdermin slinky-like oligomer== | |||
<StructureSection load='8sl0' size='340' side='right'caption='[[8sl0]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8sl0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vitiosangium_sp._GDMCC_1.1324 Vitiosangium sp. GDMCC 1.1324]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8SL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8SL0 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]] 3.3Å</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=8sl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8sl0 OCA], [https://pdbe.org/8sl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8sl0 RCSB], [https://www.ebi.ac.uk/pdbsum/8sl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8sl0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/GSDM_VITXG GSDM_VITXG] Precursor of a pore-forming protein involved in defense against bacteriophages (By similarity). Expression of bGSDM and the neighboring protease gene (Ga0334635_1659) is toxic in E.coli (PubMed:35025633). Cleavage of this precursor by its dedicated protease releases the active moiety (gasdermin bGSDM, N-terminus) which inserts into membranes, forming pores and triggering cell death (Probable) (PubMed:38509367).[UniProtKB:A0A0S2DNG5][UniProtKB:P0DV48]<ref>PMID:35025633</ref> <ref>PMID:38509367</ref> Pore-forming protein that causes membrane permeabilization, probably via a pyroptosis-like activity (Probable) (PubMed:38509367). Makes ring-like pores with an interior pore diameter of 200-300 Angstroms, when integrated in liposomes (PubMed:38509367).<ref>PMID:38509367</ref> <ref>PMID:38509367</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In response to pathogen infection, gasdermin (GSDM) proteins form membrane pores that induce a host cell death process called pyroptosis(1-3). Studies of human and mouse GSDM pores have revealed the functions and architectures of assemblies comprising 24 to 33 protomers(4-9), but the mechanism and evolutionary origin of membrane targeting and GSDM pore formation remain unknown. Here we determine a structure of a bacterial GSDM (bGSDM) pore and define a conserved mechanism of pore assembly. Engineering a panel of bGSDMs for site-specific proteolytic activation, we demonstrate that diverse bGSDMs form distinct pore sizes that range from smaller mammalian-like assemblies to exceptionally large pores containing more than 50 protomers. We determine a cryo-electron microscopy structure of a Vitiosangium bGSDM in an active 'slinky'-like oligomeric conformation and analyse bGSDM pores in a native lipid environment to create an atomic-level model of a full 52-mer bGSDM pore. Combining our structural analysis with molecular dynamics simulations and cellular assays, our results support a stepwise model of GSDM pore assembly and suggest that a covalently bound palmitoyl can leave a hydrophobic sheath and insert into the membrane before formation of the membrane-spanning beta-strand regions. These results reveal the diversity of GSDM pores found in nature and explain the function of an ancient post-translational modification in enabling programmed host cell death. | |||
Structure and assembly of a bacterial gasdermin pore.,Johnson AG, Mayer ML, Schaefer SL, McNamara-Bordewick NK, Hummer G, Kranzusch PJ Nature. 2024 Apr;628(8008):657-663. doi: 10.1038/s41586-024-07216-3. Epub 2024 , Mar 20. PMID:38509367<ref>PMID:38509367</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8sl0" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Vitiosangium sp. GDMCC 1 1324]] | |||
[[Category: Johnson AG]] | |||
[[Category: Kranzusch PJ]] | |||
[[Category: Mayer ML]] | |||