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

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

J Caruthers  1 , 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
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Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum

J Caruthers et al. Proteins. .

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.

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