Evolution of quaternary structure in a homotetrameric enzyme.

@article{Griffin2008EvolutionOQ,
  title={Evolution of quaternary structure in a homotetrameric enzyme.},
  author={M. D. W. Griffin and Renwick C J Dobson and Frederick Grant Pearce and Laurence Antonio and Andrew E. Whitten and Chu Kong Liew and Joel P. Mackay and Jill Trewhella and Geoffrey B Jameson and Matthew A. Perugini and Juliet A Gerrard},
  journal={Journal of molecular biology},
  year={2008},
  volume={380 4},
  pages={691-703}
}
Dihydrodipicolinate synthase (DHDPS) is an essential enzyme in (S)-lysine biosynthesis and an important antibiotic target. All X-ray crystal structures solved to date reveal a homotetrameric enzyme. In order to explore the role of this quaternary structure, dimeric variants of Escherichia coli DHDPS were engineered and their properties were compared to those of the wild-type tetrameric form. X-ray crystallography reveals that the active site is not disturbed when the quaternary structure is… CONTINUE READING

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