Journal
NATURE COMMUNICATIONS
Volume 10, Issue -, Pages -Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41467-019-11194-w
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Funding
- NIH [AR065484, R35GM122510]
- U.S. Army Medical Research Acquisition Activity (AMRAA), through the Peer Reviewed Medical Research Program (PRMRP) [W81XWH1810515]
- U.S. Department of Defense (DOD) [W81XWH1810515] Funding Source: U.S. Department of Defense (DOD)
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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 understanding of its still enigmatic function. We observe TorsinA to form helical filaments, which we analyzed by cryo-electron microscopy using helical reconstruction. The 4.4 A structure reveals long hollow tubes with a helical periodicity of 8.5 subunits per turn, and an inner channel of 4 nm diameter. We further show that the protein is able to induce tubulation of membranes in vitro, an observation that may reflect an entirely new characteristic of AAA + ATPases. We discuss the implications of these observations for TorsinA function.
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