5mlt
From Proteopedia
Structural characterization of a carbohydrate substrate binding protein from Streptococcus pneumoniae
Structural highlights
FunctionSBP92_STRPN Probably part of an ABC transporter complex involved in carbohydrate transport.[1] [2] Publication Abstract from PubMedStreptococcus 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 A 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. Structural characterization of the Streptococcus pneumoniae carbohydrate substrate-binding protein SP0092.,Culurgioni S, Tang M, Walsh MA Acta Crystallogr F Struct Biol Commun. 2017 Jan 1;73(Pt 1):54-61. doi:, 10.1107/S2053230X16020252. Epub 2017 Jan 1. PMID:28045395[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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