Structure of the MxA stalk elucidates the assembly of ring-like units of an antiviral module.

The dynamin-like MxA GTP ase (Myxovirus resistance protein 1) mediates cellular resistance against a wide range of viruses. MxA is composed of an amino-terminal G domain, a middle domain and a carboxy-terminal GTPase effector domain. We recently determined the structure of the middle domain and GTPase effector domain of MxA constituting an elongated helical stalk, and elucidated the mechanism how the stalk mediates formation of ring-like MxA oligomers. Here, we shortly review our work and discuss the MxA rings as functional units of a cellular module orchestrating and executing the antiviral response.