ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Insights into the Function and Horizontal Transfer of Isoproturon Degradation Genes (Applied and environmental microbiology · 2020Article
- Approaches to automated protein crystal harvesting.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Crystallization and preliminary X-ray diffraction analysis of selenophosphate synthetases from Trypanosoma brucei and Leishmania major.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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11 authors.
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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.
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