Atomic structures of a bacteriocin targeting Gram-positive bacteria

Atomic structures of a bacteriocin targeting Gram-positive bacteria

Blog Article

Abstract Due to envelope differences between Gram-positive and Gram-negative bacteria, engineering precision bactericidal contractile nanomachines requires atomic-level understanding of their caruso rhodiola 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 grandpas best 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.