Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1.

@article{Knegtel1996CrystalSA,
  title={Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1.},
  author={Ronald M. A. Knegtel and Rich{\`e}le D. Wind and Henriette J Rozeboom and Kor H. Kalk and Reinetta M. Buitelaar and Lubbert Dijkhuizen and Bauke W Dijkstra},
  journal={Journal of molecular biology},
  year={1996},
  volume={256 3},
  pages={
          611-22
        }
}
The crystal structure of the cyclodextrin glycosyltransferase (CGTase) from the thermophilic microorganism Thermoanaerobacterium thermosulfurigenes EM1 has been elucidated at 2.3 A resolution. The final model consists of all 683 amino acid residues, two calcium ions and 343 water molecules, and has a crystallographic R-factor of 17.9% (Rfree 24.9%) with excellent stereochemistry. The overall fold of the enzyme is highly similar to that reported for mesophilic CGTases and differences are… CONTINUE READING

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