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
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