6gy8: Difference between revisions
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==Crystal structure of XaxA from Xenorhabdus nematophila== | |||
<StructureSection load='6gy8' size='340' side='right' caption='[[6gy8]], [[Resolution|resolution]] 2.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6gy8]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GY8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GY8 FirstGlance]. <br> | |||
</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=6gy8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gy8 OCA], [http://pdbe.org/6gy8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gy8 RCSB], [http://www.ebi.ac.uk/pdbsum/6gy8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gy8 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
alpha-Xenorhabdolysins (Xax) are alpha-pore-forming toxins (alpha-PFT) that form 1-1.3 MDa large pore complexes to perforate the host cell membrane. PFTs are used by a variety of bacterial pathogens to attack host cells. Due to the lack of structural information, the molecular mechanism of action of Xax toxins is poorly understood. Here, we report the cryo-EM structure of the XaxAB pore complex from Xenorhabdus nematophila and the crystal structures of the soluble monomers of XaxA and XaxB. The structures reveal that XaxA and XaxB are built similarly and appear as heterodimers in the 12-15 subunits containing pore, classifying XaxAB as bi-component alpha-PFT. Major conformational changes in XaxB, including the swinging out of an amphipathic helix are responsible for membrane insertion. XaxA acts as an activator and stabilizer for XaxB that forms the actual transmembrane pore. Based on our results, we propose a novel structural model for the mechanism of Xax intoxication. | |||
Membrane insertion of alpha-xenorhabdolysin in near-atomic detail.,Schubert E, Vetter IR, Prumbaum D, Penczek PA, Raunser S Elife. 2018 Jul 16;7. pii: 38017. doi: 10.7554/eLife.38017. PMID:30010541<ref>PMID:30010541</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6gy8" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Raunser, S]] | |||
[[Category: Schubert, E]] | |||
[[Category: Bacterial toxin]] | |||
[[Category: Pore forming-toxin]] | |||
[[Category: Toxin]] | |||
Latest revision as of 10:24, 25 July 2018
Crystal structure of XaxA from Xenorhabdus nematophilaCrystal structure of XaxA from Xenorhabdus nematophila
Structural highlights
Publication Abstract from PubMedalpha-Xenorhabdolysins (Xax) are alpha-pore-forming toxins (alpha-PFT) that form 1-1.3 MDa large pore complexes to perforate the host cell membrane. PFTs are used by a variety of bacterial pathogens to attack host cells. Due to the lack of structural information, the molecular mechanism of action of Xax toxins is poorly understood. Here, we report the cryo-EM structure of the XaxAB pore complex from Xenorhabdus nematophila and the crystal structures of the soluble monomers of XaxA and XaxB. The structures reveal that XaxA and XaxB are built similarly and appear as heterodimers in the 12-15 subunits containing pore, classifying XaxAB as bi-component alpha-PFT. Major conformational changes in XaxB, including the swinging out of an amphipathic helix are responsible for membrane insertion. XaxA acts as an activator and stabilizer for XaxB that forms the actual transmembrane pore. Based on our results, we propose a novel structural model for the mechanism of Xax intoxication. Membrane insertion of alpha-xenorhabdolysin in near-atomic detail.,Schubert E, Vetter IR, Prumbaum D, Penczek PA, Raunser S Elife. 2018 Jul 16;7. pii: 38017. doi: 10.7554/eLife.38017. PMID:30010541[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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