High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels.

@article{Hcker2009HighresolutionCS,
  title={High-resolution crystal structure of an artificial (betaalpha)(8)-barrel protein designed from identical half-barrels.},
  author={Birte H{\"o}cker and Adriane Lochner and T. Seitz and J{\"o}rg Claren and Reinhard Sterner},
  journal={Biochemistry},
  year={2009},
  volume={48 6},
  pages={
          1145-7
        }
}
Ample evidence suggests that the ubiquitous (betaalpha)(8)-barrel enzyme fold has evolved by the duplication and fusion of an ancestral (betaalpha)(4)-half-barrel. To reconstruct this process in the laboratory with a model protein, we earlier fused two copies of the C-terminal half-barrel HisF-C of imidazole glycerol phosphate synthase (HisF) and stepwise stabilized the resulting HisF-CC construct. We now further increased its stability and solubility by introducing two additional amino acid… CONTINUE READING

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