Stabilisation of a (βα)8-barrel protein designed from identical half barrels

@inproceedings{Seitz2007StabilisationOA,
  title={Stabilisation of a (βα)8-barrel protein designed from identical half barrels},
  author={T. Seitz and Marco Bocola and J{\"o}rg Claren and Reinhard Sterner},
  year={2007}
}
It has been suggested that the common (βα)8-barrel enzyme fold has evolved by the duplication and fusion of identical (βα)4-half barrels, followed by the optimisation of their interface. In our attempts to reconstruct these events in vitro we have previously linked in tandem two copies of the C-terminal half barrel HisF-C of imidazole glycerol phosphate synthase from Thermotoga maritima and subsequently reconstituted in the fusion construct HisF-CC a salt bridge cluster present in wild-type… CONTINUE READING

Citations

Publications citing this paper.
SHOWING 1-10 OF 12 CITATIONS

Establishing wild-type levels of catalytic activity on natural and artificial (beta alpha)8-barrel protein scaffolds.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 2009
VIEW 8 EXCERPTS
CITES BACKGROUND