Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution.

@article{Okada1997ThreedimensionalSO,
  title={Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution.},
  author={Keiji Okada and Ken Hirotsu and Michihiko Sato and Hideyuki Hayashi and Hiroyuki Kagamiyama},
  journal={Journal of biochemistry},
  year={1997},
  volume={121 4},
  pages={637-41}
}
The X-ray crystallographic structure of the branched-chain amino acid aminotransferase from Escherichia coli was determined by means of isomorphous replacement using the selenomethionyl enzyme as one of the heavy atom derivatives. The enzyme is a homo hexamer with D3 symmetry, and the polypeptide chain of the subunit is folded into two domains (small and large domains). The coenzyme, pyridoxal 5'-phosphate, resides at the domain interface, its re-face facing toward the protein. The active site… CONTINUE READING

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