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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28 Citations
Highly Influential Citations
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Background Citations
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Methods Citations
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28 Citations

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Catalytic residues and an electrostatic sandwich that promote enolpyruvyl shikimate 3-phosphate synthase (AroA) catalysis.
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Crystal structure of 5-enolpyruvylshikimate-3-phosphate synthase from a psychrophilic bacterium, Colwellia psychrerythraea 34H.
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Crystal structure of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase from the ESKAPE pathogen Acinetobacter baumannii.
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Hydrogen/deuterium exchange mass spectrometry for characterizing phosphoenolpyruvate-induced structural transitions in Mycobacterium tuberculosis 5-enolpyruvylshikimate-3-phosphate synthase (EC 2.5.1.1)
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Investigation of the target-site resistance of EPSP synthase mutants P106T and T102I/P106S against glyphosate
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Structural Basis of Glyphosate Tolerance Resulting from Mutations of Pro101 in Escherichia coli 5-Enolpyruvylshikimate-3-phosphate Synthase*
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5‐Enolpyruvylshikimate‐3‐phosphate synthase from Staphylococcus aureus is insensitive to glyphosate
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Transition state analysis of enolpyruvylshikimate 3-phosphate (EPSP) synthase (AroA)-catalyzed EPSP hydrolysis.
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Characterization of a class II 5-enopyruvylshikimate-3-phosphate synthase with high tolerance to glyphosate from Sinorhizobium fredii
  • L. Wang, R. Peng, +5 authors Q. Yao
  • Biology, Medicine
  • World journal of microbiology & biotechnology
  • 2014
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References

SHOWING 1-10 OF 32 REFERENCES
Shikimate-3-phosphate binds to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase.
  • 9
5-Enolpyruvylshikimate-3-phosphate synthase of Bacillus subtilis is an allosteric enzyme. Analysis of Arg24-->Asp, Pro105-->Ser and His385-->Lys mutations suggests a hidden phosphoenolpyruvate-binding site.
  • 17
5-Enolpyruvylshikimate-3-phosphate synthase of Bacillus subtilis is an allosteric enzyme. Analysis of Arg24-->Asp, Pro105-->Ser and His385-->Lys mutations suggests a hidden phosphoenolpyruvate-binding site.
  • 15
Interaction of the herbicide glyphosate with its target enzyme 5-enolpyruvylshikimate 3-phosphate synthase in atomic detail.
  • 399
  • PDF
Structure and topological symmetry of the glyphosate target 5-enolpyruvylshikimate-3-phosphate synthase: a distinctive protein fold.
  • 129
  • PDF
Characterization of Streptococcus pneumoniae 5-enolpyruvylshikimate 3-phosphate synthase and its activation by univalent cations.
  • 32
Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA.
  • 50
Over-production of 5-enolpyruvylshikimate-3-phosphate synthase in Escherichia coli: use of the T7 promoter.
  • 19
Site-directed mutagenesis of putative active site residues of 5-enolpyruvylshikimate-3-phosphate synthase.
  • 28
Evidence for the shikimate pathway in apicomplexan parasites
  • 440
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