Rotation, structure, and classification of prokaryotic V-ATPase
Rotation, structure, and classification of prokaryotic V-ATPase
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DOI：
10.1007/s10863-005-9480-1
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发表时间：
2005-12-01
影响因子：
3
通讯作者：
Imamura, H
中科院分区：
文献类型：
--
作者：
Yokoyama, K;Imamura, H
原核V型ATP酶/合酶（原核V-ATP酶）比真核V-ATP酶具有更简单的亚基组成，因此是研究V-ATP酶化学、物理和结构特性的有用对象。本文就嗜热真杆菌V-ATPase结构与功能关系的研究进展作一综述。首先，我们描述了嗜热T.thermophilus V-ATPase的单分子分析。使用单分子技术，它被确定为V-ATPase是一个旋转马达。其次，我们讨论了V-ATP酶亚基的排列。第三，C-亚基（真核生物D-亚基的同源物）的晶体结构进行了描述。这个漏斗形亚基似乎覆盖了V-0结构域中的蛋白脂质环，以容纳V-1中心柄。这种结构对于V-1和V-0结构域的调节可逆缔合/解离似乎是必不可少的。最后讨论了V-ATPase家族的分类。我们建议使用术语原核V-ATP酶，而不是术语古型ATP酶（A-ATP酶）。
The prokaryotic V-type ATPase/synthases (prokaryotic V-ATPases) have simpler subunit compositions than eukaryotic V-ATPases, and thus are useful subjects for studying chemical, physical and structural properties of V-ATPase. In this review, we focus on the results of recent studies on the structure/function relationships in the V-ATPase from the eubacterium Thermus thermophilus. First, we describe single-molecule analyses of T.thermophilus V-ATPase. Using the single-molecule technique, it was established that the V-ATPase is a rotary motor. Second, we discuss arrangement of subunits in V-ATPase. Third, the crystal structure of the C-subunit (homolog of eukaryotic d-subunit) is described. This funnel-shape Subunit appears to cap the proteolipid ring in the V-0 domain in order to accommodate the V-1 central stalk. This structure seems essential for the regulatory reversible association/dissociation of the V-1 and the V-0 domains. Last, we discuss classification of the V-ATPase family. We propose that the term prokaryotic V-ATPases should be used rather than the term archaeal-type ATPase (A-ATPase).