4GMK

Crystal Structure of Ribose 5-Phosphate Isomerase from the Probiotic Bacterium Lactobacillus salivarius UCC118

Summary for 4GMK

• Entry DOI: 10.2210/pdb4gmk/pdb
• Descriptor: Ribose-5-phosphate isomerase A, PHOSPHATE ION, POTASSIUM ION, ... (4 entities in total)
• Functional Keywords: d-ribose-5-phosphate isomerase family, ribose 5-phosphate isomerisation, isomerase
• Biological source: Lactobacillus salivarius
• Total number of polymer chains: 2
• Total formula weight: 50201.40

Authors

Lobley, C.M.C.,Aller, P.,Douangamath, A.,Reddivari, Y.,Bumann, M.,Bird, L.E.,Brandao-Neto, J.,Owens, R.J.,O'Toole, P.W.,Walsh, M.A. (deposition date: 2012-08-16, release date: 2012-08-29, Last modification date: 2024-02-28)

Primary citation

Lobley, C.M.,Aller, P.,Douangamath, A.,Reddivari, Y.,Bumann, M.,Bird, L.E.,Nettleship, J.E.,Brandao-Neto, J.,Owens, R.J.,O'Toole, P.W.,Walsh, M.A.
Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118.
Acta Crystallogr.,Sect.F, 68:1427-1433, 2012

PubMed 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.

PubMed: 23192019
DOI: 10.1107/S174430911204273X

Experimental method

X-RAY DIFFRACTION (1.72 Å)