1j3p

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1j3p, resolution 2.02Å

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Crystal structure of Thermococcus litoralis phosphoglucose isomerase

Overview

The gene encoding phosphoglucose isomerase was cloned from Thermococcus, litoralis, and functionally expressed in Escherichia coli. The purified, enzyme, a homodimer of 21.5 kDa subunits, was biochemically characterized., The inhibition constants for four competitive inhibitors were determined., The enzyme contained 1.25 mol Fe and 0.24 mol Zn per dimer. The activity, was enhanced by the addition of Fe(2+), but inhibited by Zn(2+) and EDTA., Enzymes with mutations in conserved histidine and glutamate residues in, their cupin motifs contained no metals, and showed large decreases in, k(cat). The circular dichroism spectra of the mutant enzymes and the wild, type enzyme were essentially the same but with slight differences.

About this Structure

1J3P is a Single protein structure of sequence from Thermococcus litoralis with FE as ligand. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.

Reference

Characterization of the cupin-type phosphoglucose isomerase from the hyperthermophilic archaeon Thermococcus litoralis., Jeong JJ, Fushinobu S, Ito S, Jeon BS, Shoun H, Wakagi T, FEBS Lett. 2003 Jan 30;535(1-3):200-4. PMID:12560104

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