1KS2

Crystal Structure Analysis of the rpiA, Structural Genomics, protein EC1268.

Summary for 1KS2

• Entry DOI: 10.2210/pdb1ks2/pdb
• Descriptor: protein EC1268, RPIA (2 entities in total)
• Functional Keywords: structural genomics, isomerase, psi, protein structure initiative, midwest center for structural genomics, mcsg
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 46329.42

Authors

Zhang, R.,Joachimiak, A.,Edwards, A.M.,Skarina, T.,Savchenko, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2002-01-10, release date: 2002-08-14, Last modification date: 2017-10-11)

Primary citation

Zhang, R.,Andersson, C.E.,Savchenko, A.,Skarina, T.,Evdokimova, E.,Beasley, S.,Arrowsmith, C.H.,Edwards, A.M.,Joachimiak, A.,Mowbray, S.L.
Structure of Escherichia coli ribose-5-phosphate isomerase: a ubiquitous enzyme of the pentose phosphate pathway and the Calvin cycle.
STRUCTURE, 11:31-42, 2003

PubMed 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 A 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 A resolution. A mechanism for acid-base catalysis is proposed.

PubMed: 12517338
DOI: 10.1016/S0969-2126(02)00933-4

Experimental method

X-RAY DIFFRACTION (1.5 Å)