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Structural characterization of the PTS IIA and IIB proteins associated with pneumococcal fucose utilization
Author(s) -
Higgins Melanie A.,
Hamilton Aileen M.,
Boraston Alisdair B.
Publication year - 2017
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.25264
Subject(s) - fucose , operon , streptococcus pneumoniae , phosphotransferase , transporter , biochemistry , permease , glucose transporter , biology , bacteria , gene , microbiology and biotechnology , computational biology , chemistry , glycoprotein , genetics , escherichia coli , insulin
Streptococcus pneumoniae harbors a significant number of transporters, including phosphotransferase (PTS) systems, allowing the bacterium to utilize a number of different carbohydrates for metabolic and other purposes. The genes encoding for one PTS transport system in particular (EII fuc ) are found within a fucose utilization operon in S. pneumoniae TIGR4. Here, we report the three‐dimensional structures of IIA fuc and IIB fuc providing evidence that this PTS system belongs to the EII man family. Additionally, the predicted metabolic pathway for this distinctive fucose utilization system suggests that EII fuc transports the H‐disaccharide blood group antigen, which would represent a novel PTS transporter specificity. Proteins 2017; 85:963–968. © 2016 Wiley Periodicals, Inc.