5G5Y

S.pneumoniae ABC-transporter substrate binding protein FusA apo structure

Summary for 5G5Y

• Entry DOI: 10.2210/pdb5g5y/pdb
• Related: 5G5Z 5G60 5G61 5G62
• Descriptor: ABC TRANSPORTER, SUBSTRATE-BINDING PROTEIN, CALCIUM ION, SULFATE ION, ... (6 entities in total)
• Functional Keywords: transport protein, fusa, substrate-binding-protein, abc-transporter, transporter, fructooligosaccharides, kestose, nystose, fructo-nystose, carbohydrate, sugar, transport, pneumoniae
• Biological source: STREPTOCOCCUS PNEUMONIAE (PNEUMOCOCCUS)
• Total number of polymer chains: 2
• Total formula weight: 114072.41

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: 2024-05-08)

Primary citation

Culurgioni, 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

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

Experimental method

X-RAY DIFFRACTION (1.73 Å)