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Structure of a ribulose 5‐phosphate 3‐epimerase from Plasmodium falciparum
Author(s) -
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.
Publication year - 2005
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.20764
Subject(s) - plasmodium falciparum , pentose phosphate pathway , structural genomics , biochemistry , enzyme , lyase , shikimate pathway , chemistry , active site , ribulose , biology , phosphate , stereochemistry , protein structure , rubisco , malaria , glycolysis , atp synthase , immunology
The crystal structure of Pfal009167AAA, a putative ribulose 5‐phosphate 3‐epimerase (PfalRPE) from Plasmodium falciparum , has been determined to 2 Å 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. Proteins 2006. © 2005 Wiley‐Liss, Inc.