National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM122510
United States
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)
AR065484
United States
Citation
Journal: Nat Commun / Year: 2019 Title: The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn. Authors: F Esra Demircioglu / Weili Zheng / Alexander J McQuown / Nolan K Maier / Nicki Watson / Iain M Cheeseman / Vladimir Denic / Edward H Egelman / Thomas U Schwartz / Abstract: 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 ...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 Å 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.
History
Deposition
Apr 9, 2019
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Header (metadata) release
Jun 5, 2019
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Map release
Jul 24, 2019
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Update
Dec 11, 2019
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Current status
Dec 11, 2019
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
Name: Torsin-1A / type: protein_or_peptide / ID: 1 / Number of copies: 25 / Enantiomer: LEVO EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
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