+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-20076 | |||||||||
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Title | Cryo-EM structure of human TorsinA filament | |||||||||
Map data | Human TorsinA filament | |||||||||
Sample |
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Function / homology | Function and homology information synaptic vesicle membrane organization / nuclear membrane organization / organelle organization / regulation of dopamine uptake involved in synaptic transmission / nuclear envelope organization / intermediate filament cytoskeleton organization / protein deneddylation / regulation of protein localization to cell surface / positive regulation of synaptic vesicle endocytosis / misfolded protein binding ...synaptic vesicle membrane organization / nuclear membrane organization / organelle organization / regulation of dopamine uptake involved in synaptic transmission / nuclear envelope organization / intermediate filament cytoskeleton organization / protein deneddylation / regulation of protein localization to cell surface / positive regulation of synaptic vesicle endocytosis / misfolded protein binding / wound healing, spreading of cells / synaptic vesicle transport / kinesin binding / chaperone cofactor-dependent protein refolding / protein localization to nucleus / ERAD pathway / chaperone-mediated protein folding / cytoskeletal protein binding / secretory granule / ATP-dependent protein folding chaperone / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / cytoplasmic vesicle membrane / neuron projection development / unfolded protein binding / Cargo recognition for clathrin-mediated endocytosis / synaptic vesicle / nuclear envelope / growth cone / nuclear membrane / response to oxidative stress / cytoskeleton / cell adhesion / endoplasmic reticulum lumen / intracellular membrane-bounded organelle / endoplasmic reticulum membrane / endoplasmic reticulum / ATP hydrolysis activity / extracellular exosome / ATP binding / identical protein binding / membrane / cytosol Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 4.4 Å | |||||||||
Authors | Zheng W / Demircioglu FE / Schwartz TU / Egelman EH | |||||||||
Funding support | United States, 2 items
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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 |
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-Structure visualization
Movie |
Movie viewer |
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Structure viewer | EM map: SurfViewMolmilJmol/JSmol |
Supplemental images |
-Downloads & links
-EMDB archive
Map data | emd_20076.map.gz | 12.1 MB | EMDB map data format | |
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Header (meta data) | emd-20076-v30.xml emd-20076.xml | 11.9 KB 11.9 KB | Display Display | EMDB header |
Images | emd_20076.png | 218 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-20076 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-20076 | HTTPS FTP |
-Related structure data
Related structure data | 6oifMC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_20076.map.gz / Format: CCP4 / Size: 27 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | Human TorsinA filament | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.169 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Sample components
-Entire : TorsinA
Entire | Name: TorsinA |
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Components |
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-Supramolecule #1: TorsinA
Supramolecule | Name: TorsinA / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Escherichia coli (E. coli) |
-Macromolecule #1: Torsin-1A
Macromolecule | 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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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 32.590248 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: GQKRSLSREA LQKDLDDNLF GQHLAKKIIL NAVFGFINNP KPKKPLTLSL HGWTGTGKNF VSKIIAENIY EGGLNSDYVH LFVATLHFP HASNITLYKD QLQLWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDLVDGVSYQ KAMFIFLSNA G AERITDVA ...String: GQKRSLSREA LQKDLDDNLF GQHLAKKIIL NAVFGFINNP KPKKPLTLSL HGWTGTGKNF VSKIIAENIY EGGLNSDYVH LFVATLHFP HASNITLYKD QLQLWIRGNV SACARSIFIF DEMDKMHAGL IDAIKPFLDY YDLVDGVSYQ KAMFIFLSNA G AERITDVA LDFWRSGKQR EDIKLKDIEH ALSVSVFNNK NSGFWHSSLI DRNLIDYFVP FLPLEYKHLK MCIRVEMQSR GY EIDEDIV SRVAEEMTFF PKEERVFSDK GCKTVFTKLD YYYDD |
-Macromolecule #2: ADENOSINE-5'-TRIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 2 / Number of copies: 25 / Formula: ATP |
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Molecular weight | Theoretical: 507.181 Da |
Chemical component information | ChemComp-ATP: |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | helical reconstruction |
Aggregation state | filament |
-Sample preparation
Buffer | pH: 8 |
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Grid | Details: unspecified |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TALOS ARCTICA |
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Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 30.0 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD |
Experimental equipment | Model: Talos Arctica / Image courtesy: FEI Company |