Lobley, CMC,Aller, P,Douangamath, A,Reddivari, Y,Bumann, M,Bird, LE,Nettleship, JE,Brandao-Neto, J,Owens, RJ,O'Toole, PW,Walsh, MA

2012

January

Acta Crystallographica Section F-Structural Biology And Crystallization Communications

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

Validated

()

TUBERCULOSIS RIBOSE-5-PHOSPHATE ISOMERASE X-RAY-DIFFRACTION ESCHERICHIA-COLI D-RIBOSE-5-PHOSPHATE ISOMERASE CRYSTAL-STRUCTURE MACROMOLECULAR CRYSTALLOGRAPHY PROTEIN-CRYSTALLIZATION MOLECULAR REPLACEMENT ANGSTROM RESOLUTION MECHANISM

68

1427

1433

The structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72 angstrom resolution. The structure was solved by molecular replacement, which identified the functional homodimer in the asymmetric unit. Despite only showing 57% sequence identity to its closest homologue, the structure adopted the typical alpha and beta D-ribose 5-phosphate isomerase fold. Comparison to other related structures revealed high homology in the active site, allowing a model of the substrate-bound protein to be proposed. The determination of the structure was expedited by the use of in situ crystallization-plate screening on beamline I04-1 at Diamond Light Source to identify well diffracting protein crystals prior to routine cryocrystallo-graphy.

DOI 10.1107/S174430911204273X