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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.

Original publication

DOI

10.1107/S174430911204273X

Type

Journal article

Journal

Acta Crystallogr Sect F Struct Biol Cryst Commun

Publication Date

01/12/2012

Volume

68

Pages

1427 - 1433

Keywords

Aldose-Ketose Isomerases, Amino Acid Sequence, Binding Sites, Crystallography, X-Ray, Dimerization, Lactobacillus, Molecular Sequence Data, Protein Conformation, Protein Folding, Sequence Alignment