The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
About this item
Full title
Author / Creator
Publisher
London: Nature Publishing Group UK
Journal title
Language
English
Formats
Publication information
Publisher
London: Nature Publishing Group UK
Subjects
More information
Scope and Contents
Contents
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 ex...
Alternative Titles
Full title
The AAA + ATPase TorsinA polymerizes into hollow helical tubes with 8.5 subunits per turn
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_doaj_primary_oai_doaj_org_article_c1401ed5770944979beff084b9fa8646
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_c1401ed5770944979beff084b9fa8646
Other Identifiers
ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-019-11194-w
