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-Structure paper
タイトル | The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn. |
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ジャーナル・号・ページ | Nat Commun, Vol. 10, Issue 1, Page 3262, Year 2019 |
掲載日 | 2019年7月22日 |
著者 | F Esra Demircioglu / Weili Zheng / Alexander J McQuown / Nolan K Maier / Nicki Watson / Iain M Cheeseman / Vladimir Denic / Edward H Egelman / Thomas U Schwartz / |
PubMed 要旨 | 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. |
リンク | Nat Commun / PubMed:31332180 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 4.4 Å |
構造データ | EMDB-20076, PDB-6oif: |
化合物 | ChemComp-ATP: |
由来 |
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キーワード | HYDROLASE / AAA+ ATPase / nucleotide binding / nuclear envelope / endoplasmic reticulum / membrane |