Iino Ryota, Minagawa Yoshihiro, Ueno Hiroshi, Hara Mayu, Murata Takeshi
Department of Bioorganization Research, Okazaki Institute for Integrative Bioscience, Institute for Molecular Science, National Institutes of Natural Sciences, Aichi, Japan; Department of Functional Molecular Science, School of Physical Sciences, Graduate University for Advanced Studies (SOKENDAI), Kanagawa, Japan.
IUBMB Life. 2014 Sep;66(9):624-30. doi: 10.1002/iub.1311. Epub 2014 Sep 17.
V1-ATPase is a rotary molecular motor in which the mechanical rotation of the rotor DF subunits against the stator A3B3 ring is driven by the chemical free energy of ATP hydrolysis. Recently, using X-ray crystallography, we solved the high-resolution molecular structure of Enterococcus hirae V1-ATPase (EhV1) and revealed how the three catalytic sites in the stator A3B3 ring change their structure on nucleotide binding and interaction with the rotor DF subunits. Furthermore, recently, we also demonstrated directly the rotary catalysis of EhV1 by using single-molecule high-speed imaging and analyzed the properties of the rotary motion in detail. In this critical review, we introduce the molecular structure and rotary dynamics of EhV1 and discuss a possible model of its chemomechanical coupling scheme.
V1-ATP酶是一种旋转分子马达，其中转子DF亚基相对于定子A3B3环的机械旋转由ATP水解的化学自由能驱动。最近，我们利用X射线晶体学解析了平肠球菌V1-ATP酶（EhV1）的高分辨率分子结构，并揭示了定子A3B3环中的三个催化位点在核苷酸结合以及与转子DF亚基相互作用时如何改变其结构。此外，最近我们还通过单分子高速成像直接证明了EhV1的旋转催化作用，并详细分析了旋转运动的特性。在这篇重要综述中，我们介绍了EhV1的分子结构和旋转动力学，并讨论了其化学机械偶联机制的可能模型。
