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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 crystallographica. Section F, Structural biology and crystallization communications

Publication Date

12/2012

Volume

68

Pages

1427 - 1433

Addresses

Diamond Light Source, Harwell Science and Innovation Campus, Didcot, Oxfordshire OX11 0DE, England.

Keywords

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