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5G5Z

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

Summary for 5G5Z
Entry DOI10.2210/pdb5g5z/pdb
Related5G5Y 5G60 5G61 5G62
Related PRD IDPRD_900029
DescriptorABC TRANSPORTER, SUBSTRATE-BINDING PROTEIN, beta-D-fructofuranose-(2-1)-beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, CALCIUM ION, ... (4 entities in total)
Functional Keywordstransport protein, fusa, substrate-binding-protein, abc-transporter, transporter, fructooligosaccharides, kestose, nystose, fructo-nystose, carbohydrate, sugar, transport, pneumoniae
Biological sourceSTREPTOCOCCUS PNEUMONIAE
Total number of polymer chains4
Total formula weight227325.00
Authors
Culurgioni, S.,Harris, G.,Singh, A.K.,King, S.J.,Walsh, M.A. (deposition date: 2016-06-10, release date: 2017-01-18, Last modification date: 2024-01-10)
Primary citationCulurgioni, S.,Harris, G.,Singh, A.K.,King, S.J.,Walsh, M.A.
Structural Basis for Regulation and Specificity of Fructooligosaccharide Import in Streptococcus pneumoniae.
Structure, 25:79-93, 2017
Cited by
PubMed Abstract: 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.
PubMed: 27939783
DOI: 10.1016/j.str.2016.11.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.01 Å)
Structure validation

226707

건을2024-10-30부터공개중

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