2ate

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Image:2ate.gif

2ate, resolution 1.80Å

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Structure of the complex of PurE with NitroAIR

Overview

Structural studies, sequence alignments, and biochemistry have provided new insights into the evolution of the purine biosynthetic pathway. The importance of chemistry, the binding of ribose 5-phosphate (common to all purine biosynthetic intermediates), and transient protein-protein interactions in channeling of chemically unstable intermediates have all been examined in the past few years.

About this Structure

2ATE is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Phosphoribosylaminoimidazole carboxylase, with EC number 4.1.1.21 Full crystallographic information is available from OCA.

Reference

Modular evolution of the purine biosynthetic pathway., Kappock TJ, Ealick SE, Stubbe J, Curr Opin Chem Biol. 2000 Oct;4(5):567-72. PMID:11006546

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