ArticleActa crystallographica. Section F, Structural biology communications2017
Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092.
Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- Molecular and structural basis of oligopeptide recognition by the Ami transporter system in pneumococci.PLoS pathogens · 2024Article
- ProX from marine Synechococcus spp. show a sole preference for glycine-betaine with differential affinity between ecotypes.Environmental microbiology · 2022Article
- Article
- Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092.Journal of visualized experiments : JoVE · 2017Article
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3 authors.
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Abstract
Streptococcus pneumoniae is an opportunistic respiratory pathogen that remains a major cause of morbidity and mortality globally, with infants and the elderly at the highest risk. S. pneumoniae relies entirely on carbohydrates as a source of carbon and dedicates a third of all uptake systems to carbohydrate import. The structure of the carbohydrate-free substrate-binding protein SP0092 at 1.61 Å resolution reveals it to belong to the newly proposed subclass G of substrate-binding proteins, with a ligand-binding pocket that is large enough to accommodate complex oligosaccharides. SP0092 is a dimer in solution and the crystal structure reveals a domain-swapped dimer with the monomer subunits in a closed conformation but in the absence of carbohydrate ligand. This closed conformation may be induced by dimer formation and could be used as a mechanism to regulate carbohydrate uptake.
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