Crystal structure of rat liver betaine homocysteine s-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding.

@article{Gonzlez2004CrystalSO,
  title={Crystal structure of rat liver betaine homocysteine s-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding.},
  author={Beatriz Gonz{\'a}lez and Mar{\'i}a Angeles Pajares and Mart{\'i}n Mart{\'i}nez-Ripoll and Tom L. Blundell and Julia Sanz-Aparicio},
  journal={Journal of molecular biology},
  year={2004},
  volume={338 4},
  pages={771-82}
}
Betaine homocysteine S-methyltransferase (BHMT) is one of the two enzymes known to methylate homocysteine to generate methionine in the liver. It presents a Zn(2+) atom linked to three essential Cys residues. The crystal structure of rat liver BHMT has been solved at 2.5A resolution, using crystals with P2(1) symmetry and 45% solvent content in the cell. The asymmetric unit contains the whole functional tetramer showing point symmetry 222. The overall fold of the subunit consists mostly of a… CONTINUE READING
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Crystallization and preliminary X-ray crystallographic studies of recombinant human betaine-homocysteine S-methyltransferase

  • N. Bose, C. Momany
  • Acta Crystallog. sect. D,
  • 2001

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