Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.

@article{Lytle2001SolutionSO,
  title={Solution structure of a type I dockerin domain, a novel prokaryotic, extracellular calcium-binding domain.},
  author={Betsy L Lytle and Brian F Volkman and William M. Westler and Mark Heckman and Jin Hong Wu},
  journal={Journal of molecular biology},
  year={2001},
  volume={307 3},
  pages={745-53}
}
The type I dockerin domain is responsible for incorporating its associated glycosyl hydrolase into the bacterial cellulosome, a multienzyme cellulolytic complex, via its interaction with a receptor domain (cohesin domain) of the cellulosomal scaffolding subunit. The highly conserved dockerin domain is characterized by two Ca(2+)-binding sites with sequence similarity to the EF-hand motif. Here, we present the three-dimensional solution structure of the 69 residue dockerin domain of Clostridium… CONTINUE READING

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