5g60

S.pneumoniae ABC-transporter substrate binding protein FusA in complex with nystose

spinqualitylabelsall models 5g60, resolution 1.99Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5g60 is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, CL, GOL, NYT Related: 5g5y, 5g5z, 5g61, 5g62 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Streptococcus pneumoniae is dependent on carbohydrate uptake for colonization and pathogenesis, and dedicates over a third of its transport systems to their uptake. The ability of the pneumococcus to utilize fructooligosaccharides (FOSs) is attributed to the presence of one of two types of FOS ATP-binding cassette (ABC) transporters. Strains encoding SfuABC are only able to utilize short-chain FOSs, while strains encoding FusABC can utilize both short- and long-chain FOSs. The crystal structures of the substrate-binding protein FusA in its open and closed conformations bound to FOSs, and solution scattering data of SfuA, delineate the structural basis for import of short- and long-chain FOSs. The structure of FusA identifies an EF hand-like calcium-binding motif. This is shown to be essential for translocation of FOSs in FusABC and forms the basis for the definition of a new class of substrate-binding proteins that regulate substrate translocation by calcium. Structural Basis for Regulation and Specificity of Fructooligosaccharide Import in Streptococcus pneumoniae.,Culurgioni S, Harris G, Singh AK, King SJ, Walsh MA Structure. 2017 Jan 3;25(1):79-93. doi: 10.1016/j.str.2016.11.008. Epub 2016 Dec , 8. PMID:27939783 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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