Human phosphoglucose isomerase: expression, purification, crystallization and preliminary crystallographic analysis

Acta Crystallogr D Biol Crystallogr. 2001 Apr;57(Pt 4):592-5. doi: 10.1107/s0907444901001238.

Abstract

Phosphoglucose isomerase (PGI) is the second enzyme in the glycolytic pathway and catalyzes an aldose-ketose isomerization. Outside the cell, PGI has been found to function as both a cytokine and as a growth factor. The human pgi gene was cloned and the expressed enzyme was purified to homogeneity. Isomorphous crystals were obtained under two conditions and belong to the P2(1)2(1)2(1) space group, with unit-cell parameters a = 80.37, b = 107.54, c = 270.33 A. A 94.7% complete data set was obtained and processed to a limiting resolution of 2.6 A. The asymmetric unit contains two hPGI dimers according to density calculations, a self-rotation function map and molecular-replacement solution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Crystallization
  • Crystallography, X-Ray
  • Escherichia coli
  • Glucose-6-Phosphate Isomerase / biosynthesis
  • Glucose-6-Phosphate Isomerase / chemistry*
  • Glucose-6-Phosphate Isomerase / genetics
  • Glucose-6-Phosphate Isomerase / isolation & purification*
  • Humans
  • Models, Molecular
  • Multienzyme Complexes / biosynthesis
  • Multienzyme Complexes / chemistry
  • Multienzyme Complexes / genetics
  • Multienzyme Complexes / isolation & purification
  • Polymerase Chain Reaction
  • Protein Conformation
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

  • Multienzyme Complexes
  • Recombinant Proteins
  • Glucose-6-Phosphate Isomerase