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Nature:酵母 V-ATP酶的转动状态

摘要 : 这项研究采用低温电镜来确定一种真核V-ATP酶的三个主要转动状态的结构,让我们首次对在旋转催化过程中发生的构形变化有所认识。

 这项研究采用低温电镜来确定一种真核V-ATP酶的三个主要转动状态的结构,让我们首次对在旋转催化过程中发生的构形变化有所认识。V-ATP酶是旋转酶,利用ATP水解所释放的能量来将质子泵输穿过一个脂质双层,从而控制很多细胞内腔室的pH值。来自酿酒酵母的这种酶的三个结构显示了几个大的构形变化,它们可以解释这种ATP酶的可溶催化区域的转动是怎样与结合到膜上的、能够对质子进行转位的区域耦合在一起的。这些结构还显示,a-亚单元中的两个长的、高度倾斜的跨膜α-螺旋与c-环发生相互作用。

原文链接:

Electron cryomicroscopy observation of rotational states in a eukaryotic V-ATPase

原文摘要:

Eukaryotic vacuolar H+-ATPases (V-ATPases) are rotary enzymes that use energy from hydrolysis of ATP to ADP to pump protons across membranes and control the pH of many intracellular compartments. ATP hydrolysis in the soluble catalytic region of the enzyme is coupled to proton translocation through the membrane-bound region by rotation of a central rotor subcomplex, with peripheral stalks preventing the entire membrane-bound region from turning with the rotor. The eukaryotic V-ATPase is the most complex rotary ATPase: it has three peripheral stalks, a hetero-oligomeric proton-conducting proteolipid ring, several subunits not found in other rotary ATPases, and is regulated by reversible dissociation of its catalytic and proton-conducting regions1, 2. Studies of ATP synthases, V-ATPases, and bacterial/archaeal V/A-ATPases have suggested that flexibility is necessary for the catalytic mechanism of rotary ATPases3, 4, 5, but the structures of different rotational states have never been observed experimentally. Here we use electron cryomicroscopy to obtain structures for three rotational states of the V-ATPase from the yeast Saccharomyces cerevisiae. The resulting series of structures shows ten proteolipid subunits in the c-ring, setting the ATP:H+ ratio for proton pumping by the V-ATPase at 3:10, and reveals long and highly tilted transmembrane α-helices in the a-subunit that interact with the c-ring. The three different maps reveal the conformational changes that occur to couple rotation in the symmetry-mismatched soluble catalytic region to the membrane-bound proton-translocating region. Almost all of the subunits of the enzyme undergo conformational changes during the transitions between these three rotational states. The structures of these states provide direct evidence that deformation during rotation enables the smooth transmission of power through rotary ATPases.

来源: Nature 浏览次数:0

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