5g60 | pdb_00005g60
S.pneumoniae ABC-transporter substrate binding protein FusA in complex with nystose
Structural highlights
FunctionFUSA_STRPN Part of the ABC transporter complex FusABC-MsmK involved in short- and long-chain fructooligosaccharide (FOS) import. Required for the utilization of long-chain FOSs (PubMed:23264576). Binds kestose, nystose, fructofuranosyl-nystose and inulin, but not sucrose. Has a preference for long-chain FOSs (tetrasaccharides and larger) (PubMed:27939783).[1] [2] Publication Abstract from PubMedStreptococcus 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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