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Research article - Peer-reviewed, 2003

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


Ribose-5-phosphate isomerase A (RpiA; EC 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

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

Authors' information

Mowbray, Sherry
Swedish University of Agricultural Sciences, Department of Molecular Biosciences
Aled, Edwards
Cheryl, H Arrowsmith
Steven, Beasley
Evalena, Andersson C
Elena, Evdokimova
Andrzej, Joachimiak
Alexei, Savchenko
Tatiana, Skarina
Rong-guang, Zhang

UKÄ Subject classification

Veterinary Science
Animal and Dairy Science
Food Science

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