Structure and mechanism of vacuolar Na+-translocating ATPase from Enterococcus hirae
Structure and mechanism of vacuolar Na+-translocating ATPase from Enterococcus hirae
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DOI：
10.1007/s10863-005-9481-0
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发表时间：
2005-12-01
影响因子：
3
通讯作者：
Kakinuma, Y
中科院分区：
文献类型：
--
作者：
Murata, T;Yamato, I;Kakinuma, Y
来自海拉肠球菌的 V 型 Na+-ATP 酶由 ntp 操纵子编码的 9 种亚基 (NtpA(3).B-3、C-1、D-1、E1-3、F1-3、G(1)、I-1 和 K-10) 组成。主要亚基 A、B 和 K（蛋白脂质）的氨基酸序列与真核 V-ATP 酶的 A、B 和 c 亚基以及 F-ATP 酶的 β、α 和 c 亚基的氨基酸序列高度相似。我们利用F-ATP酶的β和α亚基的结构通过同源建模对A和B亚基进行建模，并通过X射线晶体学获得了NtpK环的原子结构。在这里，我们简要总结了 E. hirae V-ATPase 整体结构和机制的当前模型。
V-type Na+-ATPase from Entercoccus hirae consists of nine kinds of subunits (NtpA(3). B-3, C-1, D-1, E1-3, F1-3, G(1), I-1, and K-10) which are encoded by the ntp operon. The amino acid sequences of the major subunits, A, B, and K (proteolipid), were highly similar to those of A, B, and c subunits of eukaryotic V-ATPases, and those of beta, alpha, and c subunits of F-ATPases. We, modeled the A and B Subunits by homology modeling using the structure of beta and alpha subunits of F-ATPase, and obtained an atomic structure of NtpK ring by X-ray crystallography. Here we briefly summarize our Current models of the whole structure and mechanism of the E. hirae V-ATPase.