Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118
Lobley CMC., Aller P., Douangamath A., Reddivari Y., Bumann M., Bird LE., Nettleship JE., Brandao-Neto J., Owens RJ., Otoole PW., Walsh MA.
The structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72 A 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 and β 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 cryocrystallography. © 2012. © 2012 International Union of Crystallography All rights reserved.