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

DOI: 10.1107/S174430911204273X DOI Help
PMID: 23192019 PMID Help

Authors: Carina Lobley (Diamond Light Source) , Pierre Aller (Diamond Light Source) , Alice Douangamath (Diamond Light Source) , Yamini Reddivari (Oxford Protein Production Facility UK, UK) , Mario Bumann (ESRF) , Louise Bird (Research Complex at harwell) , Joanne E. Nettleship (Oxford Protein Production Facility UK, UK) , Jose Brandao-neto (Diamond Light Source) , Ray Owens (University of Oxford) , Paul W. O'toole (University College Cork, Ireland) , Martin A. Walsh (Diamond Light Source)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications , VOL 68 , PAGES 1427-1433

State: Published (Approved)
Published: December 2012

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 and 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 Keywords: Crystal Structure; Crystallization; Crystals; Diamonds; Light Sources; Phosphates; Plates; Proteins; Resolution; Screening; Substrates

Subject Areas: Biology and Bio-materials, Food Science, Medicine

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 26/11/2012 20:44

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