1VFL

Adenosine deaminase

1VFL の概要

• エントリーDOI: 10.2210/pdb1vfl/pdb
• 分子名称: Adenosine deaminase, ZINC ION (3 entities in total)
• 機能のキーワード: beta-barel, hydrolase
• 由来する生物種: Bos taurus (cattle)
• 細胞内の位置: Cell membrane; Peripheral membrane protein; Extracellular side (By similarity): P56658
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 40407.08

構造登録者

Kinoshita, T. (登録日: 2004-04-16, 公開日: 2005-08-16, 最終更新日: 2023-12-27)

主引用文献

Kinoshita, T.,Nakanishi, I.,Terasaka, T.,Kuno, M.,Seki, N.,Warizaya, M.,Matsumura, H.,Inoue, T.,Takano, K.,Adachi, H.,Mori, Y.,Fujii, T.
Structural Basis of Compound Recognition by Adenosine Deaminase
Biochemistry, 44:10562-10569, 2005

PubMed Abstract: Structural snapshots corresponding to various states enable elucidation of the molecular recognition mechanism of enzymes. Adenosine deaminase has two distinct conformations, an open form and a closed form, although it has so far been unclear what factors influence adaptation of the alternative conformations. Herein, we have determined the first nonligated structure as an initial state, which was the open form, and have thereby rationally deduced the molecular recognition mechanism. Inspection of the active site in the nonligated and ligated states indicated that occupancy at one of the water-binding positions in the nonligated state was highly significant in determining alternate conformations. When this position is empty, subsequent movement of Phe65 toward the space induces the closed form. On the other hand, while occupied, the overall conformation remains in the open form. This structural understanding should greatly assist structure-oriented drug design and enable control of the enzymatic activity.

PubMed: 16060665
DOI: 10.1021/bi050529e

実験手法

X-RAY DIFFRACTION (1.8 Å)