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Streptococcus pneumoniae is an opportunistic respiratory pathogen that remains a major cause of morbidity and mortality globally with infants and the elderly at 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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This page is a summary of: Structural characterization of theStreptococcus pneumoniaecarbohydrate substrate-binding protein SP0092, Acta Crystallographica Section F Structural Biology Communications, January 2017, International Union of Crystallography,
DOI: 10.1107/s2053230x16020252.
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