Crystal structure of Thermococcus litoralis phosphogrucose isomerase complexed with gluconate-6-phosphate

File:1j3r.jpg


1j3r, resolution 2.18Å

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OverviewOverview

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 StructureAbout this Structure

1J3R is a Single protein structure of sequence from Thermococcus litoralis with and as ligands. Active as Glucose-6-phosphate isomerase, with EC number 5.3.1.9 Full crystallographic information is available from OCA.

ReferenceReference

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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