5T5D
Crystal Structure of the PTS IIB protein associated with the fucose utilization operon from Streptococcus pneumoniae
Summary for 5T5D
Entry DOI | 10.2210/pdb5t5d/pdb |
Descriptor | PTS system, IIB component (2 entities in total) |
Functional Keywords | transport, transport protein |
Biological source | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
Total number of polymer chains | 1 |
Total formula weight | 18513.50 |
Authors | Higgins, M.A.,Boraston, A.B. (deposition date: 2016-08-30, release date: 2016-10-26, Last modification date: 2024-03-06) |
Primary citation | Higgins, M.A.,Hamilton, A.M.,Boraston, A.B. Structural characterization of the PTS IIA and IIB proteins associated with pneumococcal fucose utilization. Proteins, 85:963-968, 2017 Cited by PubMed Abstract: 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 ) are found within a fucose utilization operon in S. pneumoniae TIGR4. Here, we report the three-dimensional structures of IIA and IIB providing evidence that this PTS system belongs to the EII family. Additionally, the predicted metabolic pathway for this distinctive fucose utilization system suggests that EII transports the H-disaccharide blood group antigen, which would represent a novel PTS transporter specificity. Proteins 2017; 85:963-968. © 2016 Wiley Periodicals, Inc. PubMed: 28168775DOI: 10.1002/prot.25264 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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