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

FEBS Letters

Rockel, Beate¹  Baumeister, Wolfgang¹  Walz, Jochen¹  Typke, Dieter¹  Hegerl, Reiner¹  Peters, Jürgen¹ 

[1] Max-Planck-Institut für Biochemie, Abteilung für molekulare Strukturbiologie, Am Klopferspitz 18a, D-82152 Martinsried, Germany

关键词: ATPases associated with a diversity of cellular activities;    Valosine-containing protein-like ATPase from Thermoplasma acidophilum;    Electron tomography;    Thermoplasma acidophilum;    CDC48;    cell division cycle protein 48;    HEPES;    2-(4-(2-hydroxyethyl)-1-piperazinyl)-ethanesulfonic acid;    MES;    2-(N-morpholino)ethanesulfonic acid;    NSF;    N-ethylmaleimide-sensitive fusion protein;    PAGE;    polyacrylamide gel electrophoresis;    PMSF;    phenylmethylsulfonyl fluoride;    SDS;    sodium dodecyl sulfate;   

DOI  :  10.1016/S0014-5793(99)00431-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown