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Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography
Author(s) -
Rockel Beate,
Walz Jochen,
Hegerl Reiner,
Peters Jürgen,
Typke Dieter,
Baumeister Wolfgang
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00431-7
Subject(s) - thermoplasma acidophilum , aaa proteins , biology , atpase , yeast , biochemistry , microbiology and biotechnology , biophysics , enzyme
Valosine‐containing protein‐like ATPase from Thermoplasma acidophilum is a member of the superfamily of ATPases associated with a diversity of cellular activities and is closely related to CDC48 from yeast and p97 from higher eukaryotes and more distantly to N ‐ethylmaleimide‐sensitive fusion protein. We have used electron tomography to obtain low‐resolution (2–2.5 nm) three‐dimensional maps of both the whole 500 kDa complex and the N‐terminally truncated valosine‐containing protein‐like ATPase from T. acidophilum complex lacking the putative substrate binding domain.