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ヨコヤマ ケン
YOKOYAMA KEN
横山 謙 所属 京都産業大学 生命科学部 先端生命科学科 職種 教授 |
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| 言語種別 | 英語 |
| 発行・発表の年月 | 2023/07 |
| 形態種別 | 研究論文 |
| 標題 | Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase. |
| 執筆形態 | その他 |
| 掲載誌名 | Nature communications |
| 掲載区分 | 国外 |
| 巻・号・頁 | 14(1),pp.4090-4090 |
| 著者・共著者 | Atsuki Nakano,Jun-Ichi Kishikawa,Kaoru Mitsuoka,Ken Yokoyama |
| 概要 | F1 domain of ATP synthase is a rotary ATPase complex in which rotation of central γ-subunit proceeds in 120° steps against a surrounding α3β3 fueled by ATP hydrolysis. How the ATP hydrolysis reactions occurring in three catalytic αβ dimers are coupled to mechanical rotation is a key outstanding question. Here we describe catalytic intermediates of the F1 domain in FoF1 synthase from Bacillus PS3 sp. during ATP mediated rotation captured using cryo-EM. The structures reveal that three catalytic events and the first 80° rotation occur simultaneously in F1 domain when nucleotides are bound at all the three catalytic αβ dimers. The remaining 40° rotation of the complete 120° step is driven by completion of ATP hydrolysis at αDβD, and proceeds through three sub-steps (83°, 91°, 101°, and 120°) with three associated conformational intermediates. All sub-steps except for one between 91° and 101° associated with phosphate release, occur independently of the chemical cycle, suggesting that the 40° rotation is largely driven by release of intramolecular strain accumulated by the 80° rotation. Together with our previous results, these findings provide the molecular basis of ATP driven rotation of ATP synthases. |
| DOI | 10.1038/s41467-023-39742-5 |
| PMID | 37429854 |