Crystal structure of Thermococcus litoralis phosphoglucose isomeraseCrystal structure of Thermococcus litoralis phosphoglucose isomerase

Structural highlights

1j3p is a 2 chain structure with sequence from 'caldococcus litoralis' z-1301. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Activity:Glucose-6-phosphate isomerase, with EC number 5.3.1.9
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

1j3p, resolution 2.02Å

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