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ツゲ ヒデアキ
TSUGE HIDEAKI
津下 英明 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 | 2007/08 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Crystal structure of archaeal highly thermostable L-aspartate dehydrogenase/NAD/citrate ternary complex |
| 執筆形態 | その他 |
| 掲載誌名 | FEBS JOURNAL |
| 出版社・発行元 | BLACKWELL PUBLISHING |
| 巻・号・頁 | 274(16),pp.4315-4325 |
| 著者・共著者 | Kazunari Yoneda,Haruhiko Sakuraba,Hideaki Tsuge,Nobuhiko Katunuma,Toshihisa Ohshima |
| 概要 | The crystal structure of the highly thermostable L-aspartate dehydrogenase (L-aspDH; EC 1.4.1.21) from the hyperthermophilic archaeon Archaeoglobus fulgidus was determined in the presence of NAD and a substrate analog, citrate. The dimeric structure of angstrom fulgidus L-aspDH was refined at a resolution of 1.9 A with a crystallographic R-factor of 21.7% (R-free = 22.6%). The structure indicates that each subunit consists of two domains separated by a deep cleft containing an active site. Structural comparison of the A. fulgidus L-aspDH/NAD/citrate ternary complex and the Thermotoga maritima L-aspDH/NAD binary complex showed that A. fulgidus L-aspDH assumes a closed conformation and that a large movement of the two loops takes place during substrate binding. Like T. maritima L-aspDH, the A.fiulgidus enzyme is highly thermostable. But whereas a large number of inter- and intrasubunit ion pairs are responsible for the stability of A. fulgidus L-aspDH, a large number of inter- and intrasubunit aromatic pairs stabilize the T. maritima enzyme. Thus stabilization of these two L-aspDHs appears to be achieved in different ways. This is the first detailed description of substrate and coenzyme binding to L-aspDH and of the molecular basis of the high thermostability of a hyperthermophilic L-aspDH. |
| DOI | 10.1111/j.1742-4658.2007.05961.x |
| ISSN | 1742-464X |