1hp1

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spinqualitylabelsall models 1hp1, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

5'-NUCLEOTIDASE (OPEN FORM) COMPLEX WITH ATP

Overview

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.

About this Structure

1HP1 is a Single protein structure of sequence from Escherichia coli with ZN, CO3, SO4 and ATP as ligands. Full crystallographic information is available from OCA.

Reference

Mechanism of hydrolysis of phosphate esters by the dimetal center of 5'-nucleotidase based on crystal structures., Knofel T, Strater N, J Mol Biol. 2001 May 25;309(1):239-54. PMID:11491293

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