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

J. Caruthers, J. Bosch, F. Buckner, W. Van Voorhis, P. Myler, E. Worthey, C. Mehlin, E. Boni, G. DeTitta, J. Luft, A. Lauricella, O. Kalyuzhniy, L. Anderson, F. Zucker, M. Soltis, Wim G J Hol

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)338-342
Number of pages5
JournalProteins
Volume62
Issue number2
DOIs
StatePublished - Feb 1 2006
Externally publishedYes

Keywords

  • Heme detoxification
  • Malaria
  • Shikimate

ASJC Scopus subject areas

  • Genetics
  • Structural Biology
  • Biochemistry

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    Caruthers, J., Bosch, J., Buckner, F., Van Voorhis, W., Myler, P., Worthey, E., Mehlin, C., Boni, E., DeTitta, G., Luft, J., Lauricella, A., Kalyuzhniy, O., Anderson, L., Zucker, F., Soltis, M., & Hol, W. G. J. (2006). Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum. Proteins, 62(2), 338-342. https://doi.org/10.1002/prot.20764