Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases.

@article{Juers1999StructuralCO,
  title={Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases.},
  author={Douglas H Juers and Reuben E Huber and Brian W. Matthews},
  journal={Protein science : a publication of the Protein Society},
  year={1999},
  volume={8 1},
  pages={122-36}
}
Beta-galactosidase (lacZ) from Escherichia coli is a 464 kDa homotetramer. Each subunit consists of five domains, the third being an alpha/beta barrel that contains most of the active site residues. A comparison is made between each of the domains and a large set of proteins representative of all structures from the protein data bank. Many structures include an alpha/beta barrel. Those that are most similar to the alpha/beta barrel of E. coli beta-galactosidase have similar catalytic residues… CONTINUE READING
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