Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate‐bound state and S3P‐GLP‐bound state

@article{Park2004StructuralSO,
  title={Structural studies of Streptococcus pneumoniae EPSP synthase in unliganded state, tetrahedral intermediate‐bound state and S3P‐GLP‐bound state},
  author={HaJeung Park and J. L. Hilsenbeck and H. J. Kim and Wendy A. Shuttleworth and Y. Park and Jeremy N. S. Evans and C. Kang},
  journal={Molecular Microbiology},
  year={2004},
  volume={51}
}
The shikimate pathway synthesizes aromatic amino acids and other essential metabolites that are necessary for bacteria, plants and fungi to survive. This pathway is not present in vertebrates and therefore represents an attractive target for antibacterial agents. We have successfully crystallized and solved the structure of unliganded, inhibitor‐liganded and tetrahedral intermediate (TI)‐liganded forms of Streptococcus pneumoniae EPSP synthase. The overall topology of the S. pneumoniae EPSP… Expand
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