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Significance Rickettsia Sca2 mimics eukaryotic formins by promoting actin filament nucleation and elongation to assemble actin comet tails forRickettsia motility. We show that unlike formins, Sca2 is monomeric, but has N- and C-terminal repeat domains (NRD and CRD) that interact with each other. The structure of NRD reveals a new crescent-like fold. CRD is predicted to share this fold, and might form together with NRD a doughnut-shaped formin-like structure for processive elongation. Between NRD and CRD, proline-rich sequences incorporate profilin-actin for elongation, and WASP-homology 2 (WH2) domains recruit actin monomers for nucleation.Rickettsia has therefore “rediscovered” formin-like actin nucleation and elongation.

Rickettsia Sca2 has evolved formin-like activity through a different molecular mechanism