Molecular mechanism of the unidirectional rotation of the rotor-less V1 rotary motor

2019 Fiscal Year Final Research Report

• Project/Area Number: 17H03638
• Research Category: Grant-in-Aid for Scientific Research (B)
• Allocation Type: Single-year Grants
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Chiba University
• Principal Investigator: Murata Takeshi 千葉大学, 大学院理学研究院, 教授 (80415322)
• Project Period (FY): 2017-04-01 – 2020-03-31
• Keywords: V-ATPase / 分子モーター / 構造解析

Outline of Final Research Achievements

V-ATPases function as ATP-dependent ion pumps. The hydrophilic V1 portion is known as a rotary motor in which a central axis DF complex rotates inside a hexagonally arranged catalytic A3B3 complex using ATP hydrolysis energy. We previously succeeded in obtaining the crystal structures of the A3B3 complex and the dynamics showing a unidirectional rotation of the complex in the presence of ATP analog by high-speed AFM. In this study, we elucidated the crystal structures and biochemical properties of ADP bound and ATP bound A3B3 complex. Based on these and previous findings, we propose a molecular mechanism of the unidirectional rotation of the rotor-less V1 rotary motor.

Free Research Field

構造生物学

Academic Significance and Societal Importance of the Research Achievements

本研究よるA3B3複合体の分子メカニズムの解明は、V1モーターの協同的な反応機構の根本的な理解に重要であるばかりでなく、その他の分子モーターがもつ分子機構の一般原理の理解にも重要であると考えられる。また、V-ATPaseが関連するガン転移や骨粗鬆症などの重要な疾病原因の理解やその治療法についても進展することが期待される。