A novel metalloprotease family discovered through a tardigrade

Crystal structure of RvPeti from Ramazzottius varieornatus at 1.35 Å reveals a conserved His-Asp-Asp metal-binding pocket that supports Zn2+-dependent proteolytic activity.

• Why it matters: Tardigrade proteins with uncertain functions, including candidates linked to horizontal gene transfer, lack mechanistic and evolutionary characterization.
• What they did: The authors solved the RvPeti structure at 1.35 Å, used anomalous diffraction to test metal binding, and performed biochemical assays with Zn2+ and substrate panels plus chelators and residue substitutions.
• The result: RvPeti accommodates Zn2+ and Mn2+ and shows Zn2+-dependent proteolysis that is strongly reduced by a metal chelator and alanine substitutions, identifying a new metalloprotease family and enabling studies of its roles.

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