Structure of a thermophilic F1-ATPase inhibited by an ε-subunit: deeper insight into the ε-inhibition mechanism

Author:

Shirakihara Yasuo1,Shiratori Aya1,Tanikawa Hiromi1,Nakasako Masayoshi2,Yoshida Masasuke34,Suzuki Toshiharu34

Affiliation:

1. National Institute of Genetics; Mishima Japan

2. The Institute of Molecular and Cellular Biosciences; The University of Tokyo; Japan

3. The Chemical Resources Laboratory; Tokyo Institute of Technology; Yokohama Japan

4. ERATO; Japan Science and Technology Corporation (JST); Yokohama Japan

Funder

MEXT-supported Program for the Strategic Research Foundation at Private Universities, 2011-2016

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference55 articles.

1. The ATP synthase - a splendid molecular machine;Boyer;Annu Rev Biochem,1997

2. Catalytic mechanism of F1-ATPase;Weber;Biochim Biophys Acta,1997

3. ATP synthase-a marvelous rotary engine of the cell;Yoshida;Nat Rev Mol Cell Biol,2001

4. A highly stable adenosine triphosphatase from a thermophilic bacterium;Yoshida;J Biol Chem,1975

5. Structure at 2.8 Å resolution of F1-ATPase from bovine heart mitochondria;Abrahams;Nature,1994

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