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.
2005 Wiley-Liss, Inc.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Animals
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Antimalarials / chemical synthesis
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Binding Sites
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Carbohydrate Epimerases / chemistry*
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Carbohydrate Epimerases / genetics
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Carbohydrate Epimerases / isolation & purification
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Carbohydrate Epimerases / metabolism
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Cloning, Molecular
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Crystallography, X-Ray
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Drug Design
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Models, Molecular
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Plasmodium falciparum / chemistry*
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Plasmodium falciparum / genetics
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Plasmodium falciparum / isolation & purification
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Protein Folding
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Protein Structure, Secondary
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Protozoan Proteins / chemistry
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Protozoan Proteins / genetics
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Protozoan Proteins / isolation & purification
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Recombinant Proteins / chemistry
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Scattering, Radiation
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Surface Properties
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X-Ray Diffraction / methods
Substances
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Antimalarials
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Protozoan Proteins
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Recombinant Proteins
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Carbohydrate Epimerases
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ribulosephosphate 3-epimerase