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

Academic Article


  • The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 Å 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. © 2005 Wiley-Liss, Inc.
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    Author List

  • Caruthers J; Bosch J; Buckner F; Van Voorhis W; Myler P; Worthey E; Mehlin C; Boni E; DeTitta G; Luft J
  • Start Page

  • 338
  • End Page

  • 342
  • Volume

  • 62
  • Issue

  • 2