6gy6

XaxAB pore complex from Xenorhabdus nematophila

Loading... Status: waiting for Mol* initialization Structural highlights 6gy6 is a 26 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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