6GY8
Crystal structure of XaxA from Xenorhabdus nematophila
Summary for 6GY8
| Entry DOI | 10.2210/pdb6gy8/pdb |
| Descriptor | XaxA (2 entities in total) |
| Functional Keywords | bacterial toxin, pore forming-toxins, toxin |
| Biological source | Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6) |
| Total number of polymer chains | 2 |
| Total formula weight | 91189.62 |
| Authors | Schubert, E.,Raunser, S. (deposition date: 2018-06-28, release date: 2018-07-25, Last modification date: 2024-05-15) |
| Primary citation | Schubert, E.,Vetter, I.R.,Prumbaum, D.,Penczek, P.A.,Raunser, S. Membrane insertion of alpha-xenorhabdolysin in near-atomic detail. Elife, 7:-, 2018 Cited by PubMed Abstract: α-Xenorhabdolysins (Xax) are α-pore-forming toxins (α-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 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 α-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. PubMed: 30010541DOI: 10.7554/eLife.38017 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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