Open AccessStructure of ribose 5‐phosphate isomerase from Plasmodium falciparum
Author(s) -
Boni Erica,
Luft Joseph,
Holmes Margaret A.,
Buckner Frederick S.,
Van Voorhis Wesley C.,
Verlinde Christophe L. M. J.,
Mehlin Christopher,
DeTitta George,
Lauricella Angela,
Anderson Lori,
Kalyuzhniy Oleksandr,
Zucker Frank,
Schoenfeld Lori W.,
Earnest Thomas N.,
Hol Wim G. J.,
Merritt Ethan A.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106010876
Subject(s) - isomerase , pentose phosphate pathway , plasmodium falciparum , ribose , biochemistry , enzyme , chemistry , phosphate , triosephosphate isomerase , biology , glycolysis , malaria , immunology
The structure of ribose 5‐phosphate isomerase from Plasmodium falciparum , PFE0730c, has been determined by molecular replacement at 2.09 Å resolution. The enzyme, which catalyzes the isomerization reaction that interconverts ribose 5‐phosphate and ribulose 5‐phosphate, is a member of the pentose phosphate pathway. The P. falciparum enzyme belongs to the ribose 5‐phosphate isomerase A family, Pfam family PF06562 (DUF1124), and is structurally similar to other members of the family.