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Domain-domain interaction of Cu+-transporting ATPase

Research Project

Project/Area Number 22770131
Research Category

Grant-in-Aid for Young Scientists (B)

Allocation TypeSingle-year Grants
Research Field Functional biochemistry
Research InstitutionGakushuin University

Principal Investigator

TSUDA Takeo  学習院大学, 理学部, 助教 (10345233)

Project Period (FY) 2010 – 2011
Project Status Completed (Fiscal Year 2011)
Budget Amount *help
¥4,290,000 (Direct Cost: ¥3,300,000、Indirect Cost: ¥990,000)
Fiscal Year 2011: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2010: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Keywords生体エネルギー変換 / X線結晶構造解析 / イオン輸送ATPase / 蛋白質 / 結晶構造解析 / イオン輸送 / イオンポンプ / 結晶構造 / 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.

Report

(3 results)
  • 2011 Annual Research Report   Final Research Report ( PDF )
  • 2010 Annual Research Report

URL: 

Published: 2010-08-23   Modified: 2016-04-21  

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