奥地利科学技术研究所Leonid A. Sazanov团队报道了完整嗜热菌V/A型ATP酶的结构及其构象可塑性。该项研究成果发表在2019年8月23日出版的《科学》上。
研究人员解析了完整的嗜热菌（Thermus thermophilus）V/A型ATP酶的冷冻电镜结构，并以三种旋转状态和包含两种底物的方式重构进脂质纳米圆盘中。这些结构表明工作酶中V1和V0之间具有很大的灵活性，这是由于中心轴旋转和外围杆的阻力之间的机械竞争造成的。 研究人员还描述了二磷酸腺苷抑制释放，V1-V0扭矩传递和质子易位的细节，这与整个V型ATP酶家族相关。
研究人员表示， 在古细菌和真细菌中发现的V/ A型腺苷三磷酸酶（ATP酶）使用旋转催化机制将ATP水解或合成与穿过质膜的质子转运连接起来。它们属于V型ATP酶家族，这在整体结构上与线粒体/叶绿体F型ATP合酶不同。
附：英文原文
Title: Structure and conformational plasticity of the intact Thermus thermophilus V/A-type ATPase
Author: Long Zhou, Leonid A. Sazanov
Issue&Volume: Volume 365 Issue 6455
Abstract: V (vacuolar)/A (archaeal)-type adenosine triphosphatases (ATPases), found in archaea and eubacteria, couple ATP hydrolysis or synthesis to proton translocation across the plasma membrane using the rotary-catalysis mechanism. They belong to the V-type ATPase family, which differs from the mitochondrial/chloroplast F-type ATP synthases in overall architecture. We solved cryo–electron microscopy structures of the intact Thermus thermophilus V/A-ATPase, reconstituted into lipid nanodiscs, in three rotational states and two substates. These structures indicate substantial flexibility between V1 and Vo in a working enzyme, which results from mechanical competition between central shaft rotation and resistance from the peripheral stalks. We also describe details of adenosine diphosphate inhibition release, V1-Vo torque transmission, and proton translocation, which are relevant for the entire V-type ATPase family.
DOI: 10.1126/science.aaw9144
Source: https://science.sciencemag.org/content/365/6455/eaaw9144