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  Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography

Rockel, B., Walz, J., Hegerl, R., Peters, J., Typke, D., & Baumeister, W. (1999). Structure of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum as studied by electron tomography. FEBS Letters, 451(1), 27-32.

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Genre: Journal Article
Alternative Title : FEBS Lett

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 Creators:
Rockel, B.1, Author              
Walz, J.1, Author              
Hegerl, R.1, Author              
Peters, J.1, Author              
Typke, D.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Atpases associated with a diversity of cellular; Activities; Valosine-containing protein-like atpase from; Thermoplasma acidophilum; Electron tomography; Thermoplasma acidophilum.; Sensitive fusion protein; Saccharomyces-cerevisiae; Vesicular transport; Crystal-structure; Membrane-fusion; Cell-cycle; Domain; Nsf; Microscopy; Family.; Biochemistry & Biophysics in Current Contents(R)/Life Sciences.
 Abstract: 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. (C) 1999 Federation of European Biochemical Societies. [References: 35]

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 Dates: 1999
 Publication Status: Published in print
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 Identifiers: eDoc: 318648
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Title: FEBS Letters
  Alternative Title : FEBS Lett
Source Genre: Journal
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Pages: - Volume / Issue: 451 (1) Sequence Number: - Start / End Page: 27 - 32 Identifier: -