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spinqualitylabelsall models 1rao, resolution 1.56Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF E. COLI HPPK WITH AMP AND 6-HYDROXYMETHYLPTERIN-DIPHOSPHATE AT 1.56 ANGSTROM RESOLUTION

Overview

6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the, Mg(2+)-dependent pyrophosphoryl transfer from ATP to, 6-hydroxymethyl-7,8-dihydropterin (HP). The reaction follows a bi-bi, mechanism with ATP as the first substrate and AMP and HP pyrophosphate, (HPPP) as the two products. HPPK is a key enzyme in the folate, biosynthetic pathway and is essential for microorganisms but absent from, mammals. For the HPPK-catalyzed pyrophosphoryl transfer, a reaction, coordinate is constructed on the basis of the thermodynamic and transient, kinetic data we reported previously, and the reaction trajectory is mapped, out with five three-dimensional structures of the enzyme at various, liganded states. The five structures are apo-HPPK (ligand-free enzyme), HPPK.MgATP(analog) (binary complex of HPPK with its first substrate) and, HPPK.MgATP(analog).HP (ternary complex of HPPK with both substrates), which we reported previously, and HPPK.AMP.HPPP (ternary complex of HPPK, with both product molecules) and HPPK.HPPP (binary complex of HPPK with, one product), which we present in this study.

About this Structure

1RAO is a Single protein structure of sequence from Escherichia coli with AMP and HH2 as ligands. Active as 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase, with EC number 2.7.6.3 Full crystallographic information is available from OCA.

Reference

Reaction trajectory of pyrophosphoryl transfer catalyzed by 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase., Blaszczyk J, Shi G, Li Y, Yan H, Ji X, Structure. 2004 Mar;12(3):467-75. PMID:15016362

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