Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum

Proteins. 2006 Feb 1;62(2):338-42. doi: 10.1002/prot.20764.

Abstract

The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 A resolution. RPE represents an exciting potential drug target for developing antimalarials because it is involved in the shikimate and the pentose phosphate pathways. The structure is a classic TIM-barrel fold. A coordinated Zn ion and a bound sulfate ion in the active site of the enzyme allow for a greater understanding of the mechanism of action of this enzyme. This structure is solved in the framework of the Structural Genomics of Pathogenic Protozoa (SGPP) consortium.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Antimalarials / chemical synthesis
  • Binding Sites
  • Carbohydrate Epimerases / chemistry*
  • Carbohydrate Epimerases / genetics
  • Carbohydrate Epimerases / isolation & purification
  • Carbohydrate Epimerases / metabolism
  • Cloning, Molecular
  • Crystallography, X-Ray
  • Drug Design
  • Models, Molecular
  • Plasmodium falciparum / chemistry*
  • Plasmodium falciparum / genetics
  • Plasmodium falciparum / isolation & purification
  • Protein Folding
  • Protein Structure, Secondary
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / genetics
  • Protozoan Proteins / isolation & purification
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Scattering, Radiation
  • Surface Properties
  • X-Ray Diffraction / methods

Substances

  • Antimalarials
  • Protozoan Proteins
  • Recombinant Proteins
  • Carbohydrate Epimerases
  • ribulosephosphate 3-epimerase

Associated data

  • PDB/1TQX