Open AccessStructure of ribose 5‐phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118
Author(s) -
Lobley Carina M. C.,
Aller Pierre,
Douangamath Alice,
Reddivari Yamini,
Bumann Mario,
Bird Louise E.,
Nettleship Joanne E.,
BrandaoNeto Jose,
Owens Raymond J.,
O'Toole Paul W.,
Walsh Martin A.
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911204273x
Subject(s) - isomerase , lactobacillus salivarius , ribose , biochemistry , triosephosphate isomerase , molecular replacement , chemistry , probiotic , bacteria , biology , protein structure , enzyme , genetics
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.