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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 | 2004/01 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Crystal structure of a central stalk subunit C and reversible association/dissociation of vacuole-type ATPase |
| 執筆形態 | その他 |
| 掲載誌名 | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA |
| 出版社・発行元 | NATL ACAD SCIENCES |
| 巻・号・頁 | 101(1),pp.59-64 |
| 著者・共著者 | M Iwata,H Imamura,E Stambouli,C Ikeda,M Tamakoshi,K Nagata,H Makyio,B Hankamer,J Barber,M Yoshida,K Yokoyama,S Iwata |
| 概要 | The vacuole-type ATPases (V-ATPases) exist in various intracellular compartments of eukaryotic cells to regulate physiological processes by controlling the acidic environment. The crystal structure of the subunit C of Thermus thermophilus V-ATPase, homologous to eukaryotic subunit d of V-ATPases, has been determined at 1.95-Angstrom resolution and located into the holoenzyme complex structure obtained by single particle analysis as suggested by the results of subunit cross-linking experiments. The result shows that V-ATPase is substantially longer than the related F-type ATPase, due to the insertion of subunit C between the V-1 (soluble) and the V-o (membrane bound) domains. Subunit C, attached to the V-o. domain, seems to have a socket like function in attaching the central-stalk subunits of the V-1 domain. This architecture seems essential for the reversible association/dissociation of the V-1 and the V-o domains, unique for V-ATPase activity regulation. |
| DOI | 10.1073/pnas.0305165101 |
| ISSN | 0027-8424 |
| PMID | 14684831 |