Structural Asymmetry of F1-ATPase Caused by the γ Subunit Generates a High Affinity Nucleotide Binding Site-Reference-Cited by-同舟云学术

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Structural Asymmetry of F1-ATPase Caused by the γ Subunit Generates a High Affinity Nucleotide Binding Site

Published:1996-02 Issue:5 Volume:271 Page:2433-2438
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Kaibara Chitose,Matsui Tadashi,Hisabori Toru,Yoshida Masasuke

Funder

Hayashi Memorial Foundation for Female Natural Scientists

Grants-in-Aid for Scientific Research on Priority Areas

Ministry of Education, Science, Sports, and Culture of Japan

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference42 articles.

1. Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

2. Disulfide Bond Formation between the COOH-terminal Domain of the β Subunits and the γ and ε Subunits of the Escherichia coli F1-ATPase

3. Comparative Mg(2+)-dependent sequential covalent binding stoichiometries of 3‘-O-(4-benzoyl)benzoyl adenosine 5‘-diphosphate of MF1, TF1, and the alpha 3 beta 3 core complex of TF1. The binding change motif is independent of the F1 gamma delta epsilon subunits

4. Covalent binding of 3‘-O-(4-benzoyl)benzoyl adenosine 5‘-triphosphate (BzATP) to the isolated alpha and beta subunits and the alpha 3 beta 3 core complex of TF1. Covalent binding of BzATP prevents association of alpha and beta subunits and induces dissociation of the alpha 3 beta 3 core complex.

5. Inactivation of the bovine heart mitochondrial F1-ATPase by 5'-p-fluorosulfonylbenzoyl[3H]inosine is accompanied by modification of tyrosine 345 in a single beta subunit.

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3. Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites;Journal of Biological Chemistry;2019-01

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