Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum |
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| Authors: | 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 Wim G J |
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| Institution: | SLAC, Stanford University, Menlo Park, California, USA. |
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| 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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| Keywords: | malaria shikimate heme detoxification |
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