Literature DB >> 16682767

Structure of ribose 5-phosphate isomerase from Plasmodium falciparum.

Margaret A Holmes1, 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.   

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.

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Year:  2006        PMID： 16682767      PMCID： PMC2219984          DOI： 10.1107/S1744309106010876

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  24 in total

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Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun       Date:  2009-11-27

2.  Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118.

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6.  High-Resolution Crystal Structure of Chloroplastic Ribose-5-Phosphate Isomerase from Chlamydomonas reinhardtii-An Enzyme Involved in the Photosynthetic Calvin-Benson Cycle.

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  6 in total

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