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Research article2003Peer reviewedOpen access

Structure of Escherichia coli ribose-5-phosphate isomerase: A ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle

Zhang RG, Andersson CE, Savchenko A, Skarina T, Evdokimova E, Beasley S, Arrowsmith CH, Edwards AM, Joachimiak A, Mowbray SL

Abstract

Ribose-5-phosphate isomerase A (RpiA; EC 5.3.1.6) interconverts ribose-5-phosphate and ribulose-5-phosphate. This enzyme plays essential roles in carbohydrate anabolism and catabolism; it is ubiquitous and highly conserved. The structure of RpiA from Escherichia coli was solved by multiwavelength anomalous diffraction (MAD) phasing, and refined to 1.5 Angstrom resolution (R factor 22.4%, R-free 23.7%). RpiA exhibits an alpha/beta/(alpha/beta)/beta/alpha fold, some portions of which are similar to proteins of the alcohol dehydrogenase family. The two subunits of the dimer in the asymmetric unit have different conformations, representing the opening/closing of a cleft. Active site residues were identified in the cleft using sequence conservation, as well as the structure of a complex with the inhibitor arabinose-5-phosphate at 1.25 Angstrom resolution. A mechanism for acid-base catalysis is proposed

Published in

Structure
2003, Volume: 11, number: 1, pages: 31-42 Publisher: CELL PRESS

      SLU Authors

    • Mowbray, Sherry

      • Department of Molecular Biosciences, Swedish University of Agricultural Sciences

    UKÄ Subject classification

    Veterinary Science
    Animal and Dairy Science
    Food Science

    Publication identifier

    DOI: https://doi.org/10.1016/S0969-2126(02)00933-4

    Permanent link to this page (URI)

    https://res.slu.se/id/publ/835