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

Carina M.C. Lobley; Pierre Aller; Alice Douangamath; Yamini Reddivari; Mario Bumann; Louise E. Bird; Joanne E. Nettleship; Jose Brandao-Neto; Raymond J. Owens; Paul W. Otoole; Martin A. Walsh

doi:10.1107/S174430911204273X

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

Carina M.C. Lobley
, Pierre Aller
, Alice Douangamath
, Yamini Reddivari
, Mario Bumann
, Louise E. Bird
, Joanne E. Nettleship
, Jose Brandao-Neto
, Raymond J. Owens
, Paul W. Otoole
, Martin A. Walsh

Research output: Contribution to journal › Article › peer-review

Abstract

The structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72 A 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 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 language	English
Pages (from-to)	1427-1433
Number of pages	7
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	12
DOIs	https://doi.org/10.1107/S174430911204273X
Publication status	Published - Dec 2012

Keywords

in situ diffraction
Lactobacillus salivarius
ribose 5-phosphate isomerase

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10.1107/S174430911204273X

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Lobley, C. M. C., Aller, P., Douangamath, A., Reddivari, Y., Bumann, M., Bird, L. E., Nettleship, J. E., Brandao-Neto, J., Owens, R. J., Otoole, P. W., & Walsh, M. A. (2012). Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 68(12), 1427-1433. https://doi.org/10.1107/S174430911204273X

@article{75c5ad51a72846f393e11a58d92e474b,

title = "Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118",

abstract = "The structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72 A 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 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.",

keywords = "in situ diffraction, Lactobacillus salivarius, ribose 5-phosphate isomerase",

author = "Lobley, \{Carina M.C.\} and Pierre Aller and Alice Douangamath and Yamini Reddivari and Mario Bumann and Bird, \{Louise E.\} and Nettleship, \{Joanne E.\} and Jose Brandao-Neto and Owens, \{Raymond J.\} and Otoole, \{Paul W.\} and Walsh, \{Martin A.\}",

year = "2012",

month = dec,

doi = "10.1107/S174430911204273X",

language = "English",

volume = "68",

pages = "1427--1433",

journal = "Acta Crystallographica Section F: Structural Biology and Crystallization Communications",

issn = "1744-3091",

publisher = "John Wiley and Sons Ltd",

number = "12",

}

Lobley, CMC, Aller, P, Douangamath, A, Reddivari, Y, Bumann, M, Bird, LE, Nettleship, JE, Brandao-Neto, J, Owens, RJ, Otoole, PW & Walsh, MA 2012, 'Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118', Acta Crystallographica Section F: Structural Biology and Crystallization Communications, vol. 68, no. 12, pp. 1427-1433. https://doi.org/10.1107/S174430911204273X

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T1 - Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118

AU - Lobley, Carina M.C.

AU - Aller, Pierre

AU - Douangamath, Alice

AU - Reddivari, Yamini

AU - Bumann, Mario

AU - Bird, Louise E.

AU - Nettleship, Joanne E.

AU - Brandao-Neto, Jose

AU - Owens, Raymond J.

AU - Otoole, Paul W.

AU - Walsh, Martin A.

PY - 2012/12

Y1 - 2012/12

N2 - The structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72 A 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 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.

AB - The structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72 A 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 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.

KW - in situ diffraction

KW - Lactobacillus salivarius

KW - ribose 5-phosphate isomerase

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U2 - 10.1107/S174430911204273X

DO - 10.1107/S174430911204273X

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AN - SCOPUS:84870932740

SN - 1744-3091

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JO - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

JF - Acta Crystallographica Section F: Structural Biology and Crystallization Communications

IS - 12

ER -

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

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