4GMK

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

4GMK の概要

• エントリーDOI: 10.2210/pdb4gmk/pdb
• 分子名称: Ribose-5-phosphate isomerase A, PHOSPHATE ION, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: d-ribose-5-phosphate isomerase family, ribose 5-phosphate isomerisation, isomerase
• 由来する生物種: Lactobacillus salivarius
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 50201.40

構造登録者

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. (登録日: 2012-08-16, 公開日: 2012-08-29, 最終更新日: 2024-02-28)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.72 Å)