Article
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn.
Nature communications - 22 Jul 2019
Demircioglu F Esra, Zheng Weili, McQuown Alexander J, Maier Nolan K, Watson Nicki, Cheeseman Iain M, Denic Vladimir, Egelman Edward H, Schwartz Thomas U
Abstract excerpt
TorsinA is an ER-resident AAA + ATPase, whose deletion of glutamate E303 results in the genetic neuromuscular disease primary dystonia. TorsinA is an unusual AAA + ATPase that needs an external activator. Also, it likely does not thread a peptide substrate through a narrow central channel, in contrast to its closest structural homologs. Here, we examined the oligomerization of TorsinA to get closer to a molecular...
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