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

Structure of ribose 5‐phosphate isomerase from the probiotic bacterium Lactobacillus salivarius... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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References (53)

Publisher
Wiley
Copyright
International Union of Crystallography, 2012
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S174430911204273X
pmid
23192019
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

Acta Crystallographica Section FWiley

Published: Dec 1, 2012

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