InterPro domain: IPR036181

The MIT domain forms an asymmetric three-helix bundle. It is found in vacuolar sorting proteins, spastin (probable ATPase involved in the assembly or function of nuclear protein complexes), and a sorting nexin, which may play a role in intracellular trafficking.

A 'variant' MIT domain has been described at the N-terminal region of a related AAA-ATPase, mammalian katanin p60 [ 1 ].

This entry represents the MIT domain superfamily.

The MIT domain has a Spectrin repeat-like fold. This fold is composed of three helices in a close bundle topology. It has also a left-handed twist going up-and-down [ 2 ].

1. A common substrate recognition mode conserved between katanin p60 and VPS4 governs microtubule severing and membrane skeleton reorganization. J. Biol. Chem. 285, 16822-9
2. Structural characterization of the MIT domain from human Vps4b. Biochem. Biophys. Res. Commun. 334, 460-5