Summary for 6OIF
| Entry DOI | 10.2210/pdb6oif/pdb |
| EMDB information | 20076 |
| Descriptor | Torsin-1A, ADENOSINE-5'-TRIPHOSPHATE (2 entities in total) |
| Functional Keywords | aaa+ atpase, nucleotide binding, nuclear envelope, endoplasmic reticulum, membrane, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 25 |
| Total formula weight | 827435.72 |
| Authors | Zheng, W.,Demircioglu, F.E.,Schwartz, T.U.,Egelman, E.H. (deposition date: 2019-04-09, release date: 2019-07-24, Last modification date: 2024-11-13) |
| Primary citation | Demircioglu, F.E.,Zheng, W.,McQuown, A.J.,Maier, N.K.,Watson, N.,Cheeseman, I.M.,Denic, V.,Egelman, E.H.,Schwartz, T.U. The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn. Nat Commun, 10:3262-3262, 2019 Cited by PubMed 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 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. PubMed: 31332180DOI: 10.1038/s41467-019-11194-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.4 Å) |
Structure validation
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