8V43
CryoEM Structure of Diffocin - postcontracted - Baseplate - final state
This is a non-PDB format compatible entry.
Summary for 8V43
| Entry DOI | 10.2210/pdb8v43/pdb |
| EMDB information | 42964 |
| Descriptor | TRI-2 (CD1371), TRI-1 (CD1372), Sheath initiator (CD1370), ... (4 entities in total) |
| Functional Keywords | phage tail-like, bacteriocin, baseplate, post-contraction, virus like particle |
| Biological source | Clostridioides difficile More |
| Total number of polymer chains | 42 |
| Total formula weight | 1440211.79 |
| Authors | |
| Primary citation | Cai, X.,He, Y.,Yu, I.,Imani, A.,Scholl, D.,Miller, J.F.,Zhou, Z.H. Atomic structures of a bacteriocin targeting Gram-positive bacteria. Nat Commun, 15:7057-7057, 2024 Cited by PubMed Abstract: Due to envelope differences between Gram-positive and Gram-negative bacteria, engineering precision bactericidal contractile nanomachines requires atomic-level understanding of their structures; however, only those killing Gram-negative bacteria are currently known. Here, we report the atomic structures of an engineered diffocin, a contractile syringe-like molecular machine that kills the Gram-positive bacterium Clostridioides difficile. Captured in one pre-contraction and two post-contraction states, each structure fashions six proteins in the bacteria-targeting baseplate, two proteins in the energy-storing trunk, and a collar linking the sheath with the membrane-penetrating tube. Compared to contractile machines targeting Gram-negative bacteria, major differences reside in the baseplate and contraction magnitude, consistent with target envelope differences. The multifunctional hub-hydrolase protein connects the tube and baseplate and is positioned to degrade peptidoglycan during penetration. The full-length tape measure protein forms a coiled-coil helix bundle homotrimer spanning the entire diffocin. Our study offers mechanical insights and principles for designing potent protein-based precision antibiotics. PubMed: 39152109DOI: 10.1038/s41467-024-51038-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.1 Å) |
Structure validation
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