1HO5

5'-NUCLEOTIDASE (E. COLI) IN COMPLEX WITH ADENOSINE AND PHOSPHATE

1HO5 の概要

• エントリーDOI: 10.2210/pdb1ho5/pdb
• 関連するPDBエントリー: 1HP1 1HPU 1ush 2ush
• 分子名称: 5'-NUCLEOTIDASE, MANGANESE (II) ION, PHOSPHATE ION, ... (5 entities in total)
• 機能のキーワード: metalloprotein, domain movement, hydrolase
• 由来する生物種: Escherichia coli
• 細胞内の位置: Periplasm: P07024
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 117499.37

構造登録者

Knoefel, T.,Straeter, N. (登録日: 2000-12-08, 公開日: 2002-03-20, 最終更新日: 2024-10-30)

主引用文献

Knofel, T.,Strater, N.
Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures.
J.Mol.Biol., 309:239-254, 2001

PubMed Abstract: 5'-Nucleotidase belongs to a large superfamily of distantly related dinuclear metallophosphatases including the Ser/Thr protein phosphatases and purple acid phosphatases. The protein undergoes a 96 degrees domain rotation between an open (inactive) and a closed (active) enzyme form. Complex structures of the closed form with the products adenosine and phosphate, and with the substrate analogue inhibitor alpha,beta-methylene ADP, have been determined at 2.1 A and 1.85 A resolution, respectively. In addition, a complex of the open form of 5'-nucleotidase with ATP was analyzed at a resolution of 1.7 A. These structures show that the adenosine group binds to a specific binding pocket of the C-terminal domain. The adenine ring is stacked between Phe429 and Phe498. The N-terminal domain provides the ligands to the dimetal cluster and the conserved His117, which together form the catalytic core structure. However, the three C-terminal arginine residues 375, 379 and 410, which are involved in substrate binding, may also play a role in transition-state stabilization. The beta-phosphate group of the inhibitor is terminally coordinated to the site 2 metal ion. The site 1 metal ion coordinates a water molecule which is in an ideal position for a nucleophilic attack on the phosphorus atom, assuming an in-line mechanism of phosphoryl transfer. Another water molecule bridges the two metal ions.

PubMed: 11491293
DOI: 10.1006/jmbi.2001.4656

実験手法

X-RAY DIFFRACTION (2.1 Å)