Evolution of functional diversity in the cupin superfamily.

@article{Dunwell2001EvolutionOF,
  title={Evolution of functional diversity in the cupin superfamily.},
  author={Jim M. Dunwell and Alastair Culham and Clint E. Carter and Carlos Ruben Sosa-Aguirre and Peter W. Goodenough},
  journal={Trends in biochemical sciences},
  year={2001},
  volume={26 12},
  pages={
          740-6
        }
}
The cupin superfamily of proteins is among the most functionally diverse of any described to date. It was named on the basis of the conserved beta-barrel fold ('cupa' is the Latin term for a small barrel), and comprises both enzymatic and non-enzymatic members, which have either one or two cupin domains. Within the conserved tertiary structure, the variety of biochemical function is provided by minor variation of the residues in the active site and the identity of the bound metal ion. This… CONTINUE READING
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