Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus FoF1-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure-Reference-Cited by-同舟云学术

Chemical Conformation of the Essential Glutamate Site of the c-Ring within Thermophilic Bacillus F_oF₁-ATP Synthase Determined by Solid-State NMR Based on its Isolated c-Ring Structure

Published:2022-07-29 Issue:31 Volume:144 Page:14132-14139
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Todokoro Yasuto¹²,Kang Su-Jin¹³⁴,Suzuki Toshiharu⁵,Ikegami Takahisa⁶^ORCID,Kainosho Masatsune⁷,Yoshida Masasuke⁸,Fujiwara Toshimichi¹^ORCID,Akutsu Hideo¹³⁶^ORCID

Affiliation:

1. Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita 565-0871, Japan

2. Technical Support Division, School of Science, Osaka University, 1-1 Machikaneyama-cho, Toyonaka 560-0043, Japan

3. Department of Biophysics and Chemical Biology, Seoul National University, Gwanak-Gu, Seoul 151-742, Republic of Korea

4. College of Pharmacy, Dongduk Women’s University, Seoul 02748, Republic of Korea

5. Laboratory for Chemistry and Life Science, Institute of Innovative Research, Tokyo Institute of Technology, Midori-ku, Yokohama 226-0026, Japan

6. Graduate School of Medical Life Science, Yokohama City University, 1-7-29 Suehirocho, Tsurumi-ku, Yokohama 230-0045, Japan

7. Department of Chemistry, Graduate School of Science, Tokyo Metropolitan University, 1-1 Minami-Osawa, Hachioji, Tokyo 192-0397, Japan

8. Department of Molecular Bioscience, Kyoto Sangyo University, Kamigamo-Motoyama, Kyoto 603-8555, Japan

Funder

Ministry of Education, Culture, Sports, Science and Technology

National Research Foundation of Korea

Japan Society for the Promotion of Science

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.2c03580

Reference46 articles.

1. ATP synthase — a marvellous rotary engine of the cell

2. Structure and Mechanisms of F-Type ATP Synthases

3. Cryo-EM structures of the autoinhibited E. coli ATP synthase in three rotational states

4. Cryo-EM reveals distinct conformations of E. coli ATP synthase on exposure to ATP

5. Structure of a bacterial ATP synthase

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