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Structure of ribose 5-phosphate isomerase from Plasmodium falciparum

  • Margaret A. Holmes
  • , Frederick S. Buckner
  • , Wesley C. Van Voorhis
  • , Christophe L.M.J. Verlinde
  • , Christopher Mehlin
  • , Erica Boni
  • , George DeTitta
  • , Joseph Luft
  • , Angela Lauricella
  • , Lori Anderson
  • , Oleksandr Kalyuzhniy
  • , Frank Zucker
  • , Lori W. Schoenfeld
  • , Thomas N. Earnest
  • , Wim G.J. Hol
  • , Ethan A. Merritt
  • University of Washington
  • Hauptman-Woodward Medical Research Institute, Inc.
  • Lawrence Berkeley National Laboratory

Research output: Contribution to journalArticlepeer-review

14 Scopus citations

Abstract

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.

Original languageEnglish
Pages (from-to)427-431
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume62
Issue number5
DOIs
StatePublished - May 2006

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