Crystal structure of the central axis DF complex of the prokaryotic V-ATPase
Crystal structure of the central axis DF complex of the prokaryotic V-ATPase
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DOI：
10.1073/pnas.1108810108
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发表时间：
2011-12-13
影响因子：
11.1
通讯作者：
Murata, Takeshi
中科院分区：
文献类型：
--
作者：
Saijo, Shinya;Arai, Satoshi;Murata, Takeshi
在生物体的各种膜系统中，V-ATPase作为依赖于ATP的离子泵发挥作用。ATP水解物引起中央转子复合体的旋转，中央转子复合体由中心轴D亚基和由F和d亚基连接的膜c环组成。在这里，我们测定了2.0埃分辨率下，希雷肠球菌原核V-ATPase的df复合体的晶体结构。D亚基的结构包括一个长的左手螺旋线圈和一个独特的短β-发夹区域，该区域有效地刺激V-1-ATPase的ATPase活性两倍。F亚基与D亚基的中间部分结合。F亚基的C-末端螺旋被认为是一个调节区，通过延伸到催化的A(3)B(3)复合体中，通过形成三螺旋束与D亚基紧密结合。D和F亚基都是结合连接到c环的d亚基所必需的。根据这些发现，我们对V-ATPase的整个转子复合体(DFDC环)进行了建模。
V-ATPases function as ATP-dependent ion pumps in various membrane systems of living organisms. ATP hydrolysis causes rotation of the central rotor complex, which is composed of the central axis D subunit and a membrane c ring that are connected by F and d subunits. Here we determined the crystal structure of the DF complex of the prokaryotic V-ATPase of Enterococcus hirae at 2.0-angstrom resolution. The structure of the D subunit comprised a long left-handed coiled coil with a unique short beta-hairpin region that is effective in stimulating the ATPase activity of V-1-ATPase by twofold. The F subunit is bound to the middle portion of the D subunit. The C-terminal helix of the F subunit, which was believed to function as a regulatory region by extending into the catalytic A(3)B(3) complex, contributes to tight binding to the D subunit by forming a three-helix bundle. Both D and F subunits are necessary to bind the d subunit that links to the c ring. From these findings, we modeled the entire rotor complex (DFdc ring) of V-ATPase.