Structural Biology

The mechanics of severing microtubules

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Science  01 Sep 2017:
Vol. 357, Issue 6354, pp. 883-884
DOI: 10.1126/science.357.6354.883-b

Microtubules are stiff protein polymers that play an important role in many dynamic cellular processes. Forming and maintaining complex arrays of microtubules requires a suite of enzymes, including those that sever microtubules. Microtubule-severing enzymes belong to the large family of AAA adenosine triphosphatase (ATPase) proteins, which transduce the energy from ATP hydrolysis into mechanical force. Recent structural studies have provided insight into the inner workings of this enzyme family. Zehr et al. add to these studies by reporting the x-ray structure of a monomeric AAA domain from the microtubule-severing protein katenin and cryo-electron microscopy reconstructions of the hexamer in two conformations. The ATP occupancy of a boundary subunit drives conformational changes that result in cycling between an open spiral and a closed ring, providing the force to disrupt microtubules.

Nat. Struct. Mol. Biol. 10.1038/nsmb.3448 (2017).

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