Rockel B, Walz J, Hegerl R, Peters J, Typke D, Baumeister W
Max-Planck-Institut für Biochemie, Abteilung für molekulare Strukturbiologie, Martinsried, Germany.
FEBS Lett. 1999 May 14;451(1):27-32. doi: 10.1016/s0014-5793(99)00431-7.
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.
嗜酸热原体中含缬酪肽蛋白样ATP酶是与多种细胞活动相关的ATP酶超家族成员，与酵母中的CDC48及高等真核生物中的p97密切相关，与N - 乙基马来酰亚胺敏感融合蛋白的关系则较远。我们利用电子断层扫描技术获得了整个500 kDa复合物以及嗜酸热原体中缺少假定底物结合结构域的N端截短的含缬酪肽蛋白样ATP酶复合物的低分辨率（2 - 2.5纳米）三维图谱。
