Mowbray, Sherry
- Department of Molecular Biosciences, Swedish University of Agricultural Sciences
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
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