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嗜热栖热菌中CDC48/p97 ATP酶同源物VAT的结构:电子断层扫描研究

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

作者信息

Rockel B, Walz J, Hegerl R, Peters J, Typke D, Baumeister W

机构信息

Max-Planck-Institut für Biochemie, Abteilung für molekulare Strukturbiologie, Martinsried, Germany.

出版信息

FEBS Lett. 1999 May 14;451(1):27-32. doi: 10.1016/s0014-5793(99)00431-7.

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.

摘要

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。

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