Investigating the structural change mechanism commonly underlying over the ATPase family

2016 Fiscal Year Final Research Report

• Project/Area Number: 26840051
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Biophysics
• Research Institution: Yokohama City University
• Principal Investigator: Ito Yuko 横浜市立大学, 生命医科学研究科, 特任助教 (00608698)
• Research Collaborator: MASAIKE Tomoko 東京理科大学, 理学部応用生物科学科, 講師 (60406882)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: 分子動力学計算

Outline of Final Research Achievements

Enzymes of the ATPase family accomplish various functions using ATP hydrolysis energy, which is widely used in all living organisms. All proteins including this important ATPase, proceed their own reaction (function) along with the structural change. So as to understand the ATPase mechanism commonly underlying over ATPase family, the structural change of ATPase were investigated. The structural change of ATPase comprises the three different conformational changes: by ATP binding, by ATP hydrolysis, and by product release. To obtain the whole mechanism, all the steps need to be clarified. The beta subunit of F1-ATPase which has been studied extensively, was selected as representation of the ATPase family protein. Using the MD simulations, all the steps of the conformational change in the beta subunit were revealed. The mechanism obtained here was compared with that of other ATPases.

Free Research Field

生体分子のシミュレーション