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Structural basis of oligomerization and the mechano‐chemical function in dynamin‐like MxA

The interferon‐inducible dynamin‐like Myxovirus resistance protein A (MxA) GTPase is a key mediator of innate immunity against live‐threatening pathogens such as influenza viruses. It has been proposed that the middle domain and GTPase effector domain of dynamin‐like GTPases constitute a stalk region which mediates oligomerization and transmits conformational changes from the guanine‐nucleotide binding domain to the target structure. We have recently reported the crystal structure of the stalk region of MxA which folds into a four‐helical bundle. This structure tightly oligomerized in the crystals in a criss‐cross pattern involving three distinct interfaces and one loop. Mutations in each of these interaction sites interfered with native assembly, oligomerization, membrane binding and the antiviral activity of MxA. These results allowed us to propose a model for dynamin oligomerization and stimulated GTP hydrolysis that can be applied to all dynamin superfamily members. To further explore how the energy of nucleotide binding and hydrolysis can be transmitted from the G domain to the stalk, we continued our efforts to solve the full‐length structure of MxA and present our current progress on this topic.