Structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC118.
Acta Crystallogr Sect F Struct Biol Cryst Commun
; 68(Pt 12): 1427-33, 2012 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-23192019
ABSTRACT
The structure of ribose 5-phosphate isomerase from the probiotic bacterium Lactobacillus salivarius UCC188 has been determined at 1.72â
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 ß 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.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Aldose-Cetose Isomerases
/
Lactobacillus
Idioma:
En
Revista:
Acta Crystallogr Sect F Struct Biol Cryst Commun
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Reino Unido