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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 | 2009/12 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Crystal structure of A(3)B(3) complex of V-ATPase from Thermus thermophilus |
| 執筆形態 | その他 |
| 掲載誌名 | EMBO JOURNAL |
| 出版社・発行元 | NATURE PUBLISHING GROUP |
| 巻・号・頁 | 28(23),pp.3771-3779 |
| 著者・共著者 | Megan J. Maher,Satoru Akimoto,Momi Iwata,Koji Nagata,Yoshiko Hori,Masasuke Yoshida,Shigeyuki Yokoyama,So Iwata,Ken Yokoyama |
| 概要 | Vacuolar-type ATPases (V-ATPases) exist in various cellular membranes of many organisms to regulate physiological processes by controlling the acidic environment. Here, we have determined the crystal structure of the A(3)B(3) subcomplex of V-ATPase at 2.8 angstrom resolution. The overall construction of the A(3)B(3) subcomplex is significantly different from that of the alpha(3)beta(3) sub-domain in FoF1-ATP synthase, because of the presence of a protruding 'bulge' domain feature in the catalytic A subunits. The A(3)B(3) subcomplex structure provides the first molecular insight at the catalytic and non-catalytic interfaces, which was not possible in the structures of the separate subunits alone. Specifically, in the non-catalytic interface, the B subunit seems to be incapable of binding ATP, which is a marked difference from the situation indicated by the structure of the FoF1-ATP synthase. In the catalytic interface, our mutational analysis, on the basis of the A(3)B(3) structure, has highlighted the presence of a cluster composed of key hydrophobic residues, which are essential for ATP hydrolysis by V-ATPases. The EMBO Journal (2009) 28, 3771-3779. doi: 10.1038/emboj.2009.310; Published online 5 November 2009 |
| DOI | 10.1038/emboj.2009.310 |
| ISSN | 0261-4189/1460-2075 |
| PMID | 19893485 |