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

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...

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Published in:Acta crystallographica. Section F, Structural biology and crystallization communications Structural biology and crystallization communications, 2012-12, Vol.68 (12), p.1427-1433
Main Authors: Lobley, Carina M. C., Aller, Pierre, Douangamath, Alice, Reddivari, Yamini, Bumann, Mario, Bird, Louise E., Nettleship, Joanne E., Brandao-Neto, Jose, Owens, Raymond J., O'Toole, Paul W., Walsh, Martin A.
Format: Article
Language:English
Subjects:
Aldose-Ketose Isomerases - chemistry
Aldose-Ketose Isomerases - metabolism
Amino Acid Sequence
Bacteria
Binding Sites
Crystallography, X-Ray
Dimerization
Enzymes
in situ diffraction
Lactobacillus - enzymology
Lactobacillus salivarius
Molecular Sequence Data
Probiotics
Protein Conformation
Protein Folding
ribose 5-phosphate isomerase
Sequence Alignment
Structural Communications
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cited_by cdi_FETCH-LOGICAL-c5056-854fef70d9a95b46823e65efe7cef239dac41dfc64b6dcedf47124dc564381a63
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container_end_page 1433
container_issue 12
container_start_page 1427
container_title Acta crystallographica. Section F, Structural biology and crystallization communications
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creator Lobley, Carina M. C.
Aller, Pierre
Douangamath, Alice
Reddivari, Yamini
Bumann, Mario
Bird, Louise E.
Nettleship, Joanne E.
Brandao-Neto, Jose
Owens, Raymond J.
O'Toole, Paul W.
Walsh, Martin A.
description 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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ispartof Acta crystallographica. Section F, Structural biology and crystallization communications, 2012-12, Vol.68 (12), p.1427-1433
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2053-230X
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recordid cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3509960
source Open Access: PubMed Central; Wiley-Blackwell Read & Publish Collection
subjects Aldose-Ketose Isomerases - chemistry
Aldose-Ketose Isomerases - metabolism
Amino Acid Sequence
Bacteria
Binding Sites
Crystallography, X-Ray
Dimerization
Enzymes
in situ diffraction
Lactobacillus - enzymology
Lactobacillus salivarius
Molecular Sequence Data
Probiotics
Protein Conformation
Protein Folding
ribose 5-phosphate isomerase
Sequence Alignment
Structural Communications
title Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118
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