5T3U

Crystal Structure of the PTS IIA protein associated with the fucose utilization operon from Streptococcus pneumoniae

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history. 


Literature

Structural characterization of the PTS IIA and IIB proteins associated with pneumococcal fucose utilization.

Higgins, M.A., Hamilton, A.M., Boraston, A.B.

(2017) Proteins 85: 963-968

  • DOI: https://doi.org/10.1002/prot.25264
  • Primary Citation of Related Structures:  
    5T3U, 5T5D

  • 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 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.

    • Organizational Affiliation: 

    Biochemistry and Microbiology, University of Victoria, PO Box 3055 STN CSC, Victoria, British Columbia, V8W 3P6, Canada.


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PTS system, IIA component
A, B
148Streptococcus pneumoniae TIGR4Mutation(s): 0 
Gene Names: SP_2164
UniProt
Find proteins for A0A0H2US38 (Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4))
Explore A0A0H2US38 
Go to UniProtKB:  A0A0H2US38
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupA0A0H2US38
Sequence Annotations
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  • Reference Sequence
Small Molecules
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.15 Å
  • R-Value Free: 0.253 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.206 
  • Space Group: I 41 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 100.202α = 90
b = 100.202β = 90
c = 192.986γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
CrystalCleardata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2016-10-26
    Type: Initial release
  • Version 1.1: 2017-02-22
    Changes: Database references
  • Version 1.2: 2017-04-26
    Changes: Database references
  • Version 1.3: 2024-03-06
    Changes: Advisory, Data collection, Database references