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

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-12, Vol.68 (12), p.1427-1433
• Main Authors: Lobley, Carina M. C., Aller, Pierre, Douangamath, Alice, Reddivari, Yamini, Bumann, Mario, Bird, Louise E., Nettleship, Joanne E., Brandao-Neto, Jose, Owens, Raymond J., O'Toole, Paul W., Walsh, Martin A.
• Format: Article
• Language: English
• Subjects: Aldose-Ketose Isomerases - chemistry; Aldose-Ketose Isomerases - metabolism; Amino Acid Sequence; Bacteria; Binding Sites; Crystallography, X-Ray; Dimerization; Enzymes; in situ diffraction; Lactobacillus - enzymology; Lactobacillus salivarius; Molecular Sequence Data; Probiotics; Protein Conformation; Protein Folding; ribose 5-phosphate isomerase; Sequence Alignment; Structural Communications
• ISSN: 1744-3091; 1744-3091; 2053-230X
• DOI: 10.1107/S174430911204273X

The structure of ribose 5‐phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72 Å 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 α 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.