Structure of dihydropyrimidinase from Sinorhizobium meliloti CECT4114: new features in an amidohydrolase family member.

@article{MartnezRodrguez2010StructureOD,
  title={Structure of dihydropyrimidinase from Sinorhizobium meliloti CECT4114: new features in an amidohydrolase family member.},
  author={S Mart{\'i}nez-Rodr{\'i}guez and Ana Isabel Mart{\'i}nez-G{\'o}mez and Josefa Mar{\'i}a Clemente-Jim{\'e}nez and Felipe Rodr{\'i}guez-Vico and Juan Ma Garc{\'i}a-Ru{\'i}z and Francisco Javier Las Heras-V{\'a}zquez and Jose A Gavira},
  journal={Journal of structural biology},
  year={2010},
  volume={169 2},
  pages={200-8}
}
The recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114 (SmelDhp) has been characterised and its crystal structure elucidated at 1.85A. The global architecture of the protein is reminiscent of that of the amidohydrolase superfamily, consisting of two domains; an (alpha/beta)(8) TIM-like barrel domain, where the catalytic centre is located, and a smaller beta-sheet sandwich domain of unknown function. The c-terminal tails of each subunit extend toward another monomer in a… CONTINUE READING

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Crystal structure of D-hydantoinase from Bacillus stearothermophilus: insight into the stereochemistry of enantioselectivity

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