The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance.

@article{Dobson2005TheCS,
  title={The crystal structures of native and (S)-lysine-bound dihydrodipicolinate synthase from Escherichia coli with improved resolution show new features of biological significance.},
  author={Renwick C J Dobson and M. D. W. Griffin and Geoffrey B Jameson and Juliet A Gerrard},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2005},
  volume={61 Pt 8},
  pages={1116-24}
}
Dihydrodipicolinate synthase (DHDPS) mediates the key first reaction common to the biosynthesis of (S)-lysine and meso-diaminopimelate. The activity of DHDPS is allosterically regulated by the feedback inhibitor (S)-lysine. The crystal structure of DHDPS from Escherichia coli has previously been published, but to only a resolution of 2.5 A, and the structure of the lysine-bound adduct was known to only 2.94 A resolution. Here, the crystal structures of native and (S)-lysine-bound… CONTINUE READING

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