Structure of Bacillus cereus ZmaM, a peptidase-ABC transporter that secretes and activates zwittermicin A

Bacillus cereus ZmaM structure shows a central type IV ABC transporter flanked by peptidase modules that coordinate prezwittermicin export and activation into zwittermicin A.

• Why it matters: Type II prodrug peptidases are poorly understood, yet they are key to activating secreted toxins while protecting the producing bacterium.
• What they did: The authors solved the homodimeric ZmaM structure and used interface mutations to test how peptidase-module contacts affect both peptidase function and ATP hydrolysis activity.
• The result: Intermodule interface mutations impact both activities, implying peptidase and transporter modules are interdependent and enabling coordinated toxin activation with export for biotechnology use.

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