Cryo-EM structures of the YsaN ATPase reveal dodecameric and tetradecameric assemblies in the Yersinia enterocolitica T3SS

Cryo-EM structures of the Yersinia enterocolitica T3SS ATPase YsaN reveal two previously uncharacterized oligomers—a dodecamer at 3.51 [A] and a tetradecamer at 3.80 [A].

• Why it matters: The T3SS ATPase must assemble and regulate to function, but how oligomer formation and switching occur remains incompletely understood.
• What they did: The authors determined high-resolution cryo-EM structures of YsaN in both 12-mer and 14-mer states and used molecular dynamics simulations to model ATP-to-ADP transitions.
• The result: A conserved longitudinal fissure and specific N-terminal disulfide-stabilized interfaces are linked to interconversion between oligomers, while ATP hydrolysis is associated with global correlated compaction in the ADP-bound state.

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