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Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.

ABSTRACT: The structure of ribose 5-phosphate isomerase from Plasmodium falciparum, PFE0730c, has been determined by molecular replacement at 2.09 angstroms 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.

SUBMITTER: Holmes MA

PROVIDER: S-EPMC2219984 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature

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Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.

Holmes Margaret A MA Buckner Frederick S FS Van Voorhis Wesley C WC Verlinde Christophe L M J CL Mehlin Christopher C Boni Erica E DeTitta George G Luft Joseph J Lauricella Angela A Anderson Lori L Kalyuzhniy Oleksandr O Zucker Frank F Schoenfeld Lori W LW Earnest Thomas N TN Hol Wim G J WG Merritt Ethan A EA

Acta crystallographica. Section F, Structural biology and crystallization communications 20060412 Pt 5

The structure of ribose 5-phosphate isomerase from Plasmodium falciparum, PFE0730c, has been determined by molecular replacement at 2.09 angstroms 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. ...[more]

PMID: 16682767

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Structural characterization of a ribose-5-phosphate isomerase B from the pathogenic fungus Coccidioides immitis.

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