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首页> 外文期刊>Journal of Molecular Biology >Stator structure and subunit composition of the V-1/V-0 Na+-ATPase of the thermophilic bacterium Caloramator fervidus
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Stator structure and subunit composition of the V-1/V-0 Na+-ATPase of the thermophilic bacterium Caloramator fervidus

机译：嗜热细菌Caloramator fervidus V-1 / V-0 Na + -ATPase的定子结构和亚基组成

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摘要

The V-type Na+-ATPase of the thermophilic, anaerobic bacterium Caloramator fervidus was purified to homogeneity. The subunit compositions of the catalytic V-1 and membrane-embedded V-0 parts were determined and the structure of the enzyme complex was studied by electron microscopy. The V-1 headpiece consists of seven subunits present in one to three copies, and the V-0 part of two subunits in a ratio of 5:2. An analysis of over 7500 single particle images obtained by electron microscopy of the purified V1V0 enzyme complex revealed that the stalk region, connecting the V-1 and V-0 parts, contains two peripheral stalks in addition to a central stalk. One of the two is connected to the V-0 part, while the other is connected to the first via a bar-like structure that is positioned just above V-0, parallel with the plane of the membrane. Ln projection, this bar seems to contact the central stalk. The data show that the stator structure that prevents rotation of the static part of V-0 relative to V-1 in the rotary catalysis mechanism of energy coupling in ATPases/ATPsynthases is more complex than previously thought. (C) 2000 Academic Press. [References: 32]
机译：将嗜热厌氧细菌Caloramator fervidus的V型Na + -ATPase纯化至均质。确定催化的V-1和膜嵌入的V-0部分的亚基组成，并通过电子显微镜研究酶复合物的结构。 V-1头戴装置由七个子单元组成，它们以一到三个副本的形式出现，两个子单元的V-0部分的比例为5：2。通过电子显微镜对纯化的V1V0酶复合物获得的7500多个单颗粒图像进行的分析显示，连接V-1和V-0部分的茎区域除中央茎外还包含两个外围茎。两者中的一个连接到V-0部分，而另一个则通过位于V-0上方且平行于膜平面的杆状结构连接到第一部分。在Ln投影中，这根棒似乎与中央茎接触。数据表明，在ATPases / ATP合酶的能量耦合旋转催化机理中，阻止V-0静态部分相对于V-1旋转的定子结构比以前认为的更为复杂。 （C）2000学术出版社。 [参考：32]

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