Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 62, Issue 2, Pages 338-342Publisher
WILEY
DOI: 10.1002/prot.20764
Keywords
malaria; shikimate; heme detoxification
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Funding
- NIGMS NIH HHS [1P50GM64655-01] Funding Source: Medline
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The crystal structure of Pfa1009167AAA, 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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