My NCBISign In

Display Settings:

Format

Send to:

Choose Destination
    Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 May 1;62(Pt 5):427-31. Epub 2006 Apr 12.

    Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.

    Holmes MA, Buckner FS, Van Voorhis WC, Verlinde CL, Mehlin C, Boni E, DeTitta G, Luft J, Lauricella A, Anderson L, Kalyuzhniy O, Zucker F, Schoenfeld LW, Earnest TN, Hol WG, Merritt EA.

    Source

    Structural Genomics of Pathogenic Protozoa (SGPP) Consortium, USA.

    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.

    PMID:
    16682767
    [PubMed - indexed for MEDLINE]
    PMCID:
    PMC2219984
    Free PMC Article

    Images from this publication.See all images (3) Free text

    Figure 1
    Figure 3
    Figure 2

    Publication Types, MeSH Terms, Substances, Secondary Source ID, Grant Support

    Publication Types

    MeSH Terms

    Substances

    Secondary Source ID

    Grant Support

    LinkOut - more resources

    Full Text Sources

    Other Literature Sources

      Supplemental Content

      Icon for International Union of Crystallography Icon for PubMed Central

      Save items

      loading

      Related citations in PubMed

      See reviews... See all...

      Cited by 1 PubMed Central article

      Structures reported by this article

      Related information

      • Related Citations
        Calculated set of PubMed citations closely related to the selected article(s) retrieved using a word weight algorithm. Related articles are displayed in ranked order from most to least relevant, with the “linked from” citation displayed first.
      • Gene (GeneRIF)
        Gene records that have the current articles as Reference into Function citations (GeneRIFs). NLM staff reviewing the literature while indexing MEDLINE add GeneRIFs manually.
      • Protein Clusters
        Clusters of related proteins from the Protein Clusters database that cite the current articles. Sources of references in Protein Clusters include the associated Gene and Conserved Domain records as well as NCBI added citations.
      • References for this PMC Article
        Citation referenced in PubMed article. Only valid for PubMed citations that are also in PMC.
      • Taxonomy via GenBank
        Taxonomy records associated with the current articles through taxonomic information on related molecular database records (Nucleotide, Protein, Gene, SNP, Structure).
      • Domains
        Conserved Domain Database (CDD) records that cite the current articles. Citations are from the CDD source database records (PFAM, SMART).
      • Protein
        Protein translation features of primary database (GenBank) nucleotide records reported in the current articles as well as Reference Sequences (RefSeqs) that include the articles as references.
      • Structure
        Three-dimensional structure records in the NCBI Structure database for data reported in the current articles.
      • Free in PMC
        Free full text articles in PMC
      • Cited in PMC
        Full-text articles in the PubMed Central Database that cite the current articles.

      Recent activity

      Clear Turn Off Turn On

      Your browsing activity is empty.

      Activity recording is turned off.

      Turn recording back on

      See more...
      You are here: NCBI > Literature > PubMed
      Write to the Help Desk