Domain-domain interaction of Cu+-transporting ATPase

2011 Fiscal Year Final Research Report

• Project/Area Number: 22770131
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Single-year Grants
• Research Field: Functional biochemistry
• Research Institution: Gakushuin University
• Principal Investigator: TSUDA Takeo 学習院大学, 理学部, 助教 (10345233)
• Project Period (FY): 2010 – 2011
• Keywords: 生体エネルギー変換 / X線結晶構造解析 / イオン輸送ATPase

Research Abstract

Copper-transporting ATPase, CopA, is an ATP-powered ion-pump which exports excess copper ions from cytoplasm to the opposite side. The X-ray crystal structures of Ca^<2+>-ATPase, also belonging to the ion-pump family, have been determined for several different states in the reaction cycle. Comparison of these structures reveals that large rearrangements in the three cytoplasmic domains are important for ion transporting in the transmembrane helices. CopA also contains an additional N-terminal metal binding-domain(NMBD), while it is unclear the functional meaning of it. Therefore, we performed to determine the X-ray crystal structures of the complex for the cytoplasmic domains of CopA to elucidate the roles of domain-domain interactions including the NMBD for Cu-transport.