Structure of a ribulose 5-phosphate 3-epimerase from Plasmodium falciparum. Proteins 2006 Feb 01;62(2):338-42
Date
11/24/2005Pubmed ID
16304640DOI
10.1002/prot.20764Scopus ID
2-s2.0-30144441401 (requires institutional sign-in at Scopus site) 18 CitationsAbstract
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.
Author List
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 WGMESH terms used to index this publication - Major topics in bold
AnimalsAntimalarials
Binding Sites
Carbohydrate Epimerases
Cloning, Molecular
Crystallography, X-Ray
Drug Design
Models, Molecular
Plasmodium falciparum
Protein Folding
Protein Structure, Secondary
Protozoan Proteins
Recombinant Proteins
Scattering, Radiation
Surface Properties
X-Ray Diffraction
