High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases.

@article{Dobritzsch1998HighRC,
  title={High resolution crystal structure of pyruvate decarboxylase from Zymomonas mobilis. Implications for substrate activation in pyruvate decarboxylases.},
  author={Doreen Dobritzsch and Stephan K{\"o}nig and G. R. Eugenia Schneider and Gongxuan Lu},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 32},
  pages={20196-204}
}
The crystal structure of tetrameric pyruvate decarboxylase from Zymomonas mobilis has been determined at 1.9 A resolution and refined to a crystallographic R-factor of 16.2% and Rfree of 19.7%. The subunit consists of three domains, all of the alpha/beta type. Two of the subunits form a tight dimer with an extensive interface area. The thiamin diphosphate binding site is located at the subunit-subunit interface, and the cofactor, bound in the V conformation, interacts with residues from the N… CONTINUE READING

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