Published in
Wiley, Proteins: Structure, Function, and Bioinformatics, 2(62), p. 338-342, 2005
DOI: 10.1002/prot.20764
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Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum
,
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
and other authors.
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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.