5mlt

Structural characterization of a carbohydrate substrate binding protein from Streptococcus pneumoniae

spinqualitylabelsall models 5mlt, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5mlt is a 1 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.61Å Ligands: MSE, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SBP92_STRPN Probably part of an ABC transporter complex involved in carbohydrate transport. Publication Abstract from PubMed 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 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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