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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 | 2002/10 |
| 形態種別 | 研究論文 |
| 査読 | 査読あり |
| 標題 | Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-angstrom resolution: A large conformational change in ADP-dependent glucokinase |
| 執筆形態 | その他 |
| 掲載誌名 | PROTEIN SCIENCE |
| 出版社・発行元 | COLD SPRING HARBOR LAB PRESS |
| 巻・号・頁 | 11(10),pp.2456-2463 |
| 担当区分 | 筆頭著者,責任著者 |
| 著者・共著者 | H Tsuge,H Sakuraba,T Kobe,A Kujime,N Katunuma,T Ohshima |
| 概要 | Although ATP is the most common phosphoryl group donor for kinases, some kinases from certain hyperthermophilic archaea such as Pyrococcus horikoshii and Thermococcus litoralis use ADP as the phosphoryl donor. Those are ADP-dependent glucokinases (ADPGK) and phosphofructokinases in their glycolytic pathway. Here, we succeeded in gene cloning the ADPGK front P. horikoshii OT3 (phGK) in Escherichia coli,and in easy preparation of the enzyme, crystallization, and the structure determination of the apo enzyme. Recently, the three-dimensional structure of the ADPGK from T. litoralis (tIGK) in a complex with ADP was reported. The overall structure of two homologous enzymes (56.7%) was basically similar: This means that they consisted of large alpha/beta-domains and small domains. However, a marked adjustment of the two domains, which is a 10-Angstrom translation and a 20degrees rotation from the conserved GG sequence located at the center of the hinge, was observed between the apo-phGK and ADP-tIGK structures. The ADP-binding loop (430-439) was disordered in the apo form. It is suggested that a large conformational change takes place during the enzymatic reaction. |
| DOI | 10.1110/ps.0215602 |
| ISSN | 0961-8368 |