9WSZ
CryoEM structure of baseplate iris structure in the contracted AlgoCIS
Summary for 9WSZ
| Entry DOI | 10.2210/pdb9wsz/pdb |
| EMDB information | 66211 |
| Descriptor | Baseplate protein Alg12, Baseplate protein J-like domain-containing protein (2 entities in total) |
| Functional Keywords | contractile injection system, cryoem, marine bacterium, structural protein |
| Biological source | Algoriphagus machipongonensis More |
| Total number of polymer chains | 12 |
| Total formula weight | 1355578.82 |
| Authors | Xu, J.,Ericson, C.F.,Toenshoff, E.R.,Pilhofer, M. (deposition date: 2025-09-15, release date: 2026-05-06) |
| Primary citation | Xu, J.,Ericson, C.F.,Toenshoff, E.R.,Pilhofer, M. Stepwise firing mechanism of an extracellular contractile injection system. Nat Commun, 2026 Cited by PubMed Abstract: Contractile injection systems (CISs) mediate cell-cell interactions and are widespread among bacteria and archaea. These phage tail-like macromolecular machines puncture their target by a tube that is propelled by a contractile sheath. The mechanism underlying CIS firing, which starts with target binding and ends with sheath contraction, remains unclear. Here, we investigate the extracellular CIS from Algoriphagus machipongonensis (AlgoCIS) by a multimodal cryo-electron microscopy approach and structure-guided engineering, which allowed us to arrest AlgoCIS in multiple intermediate states of firing. Together with the post-firing structure, our data suggest a stepwise firing mechanism involving all structural modules: signal propagation starts with the binding of the tail-fibers, followed by opening of the cage, an expansion of the baseplate iris, and resulting in sheath contraction and the release of cap adaptor. Our study will serve as a framework for understanding the firing mechanism of diverse CISs and will facilitate the engineering of CISs for biomedical applications. PubMed: 42031783DOI: 10.1038/s41467-026-72240-y PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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