1j3p
From Proteopedia
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. 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 Page seeded by OCA on Fri May 2 20:46:05 2008
