The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins.

@article{Gurmu2009TheCS,
  title={The crystal structure of the protein YhaK from Escherichia coli reveals a new subclass of redox sensitive enterobacterial bicupins.},
  author={Daniel Gurmu and Jun Lu and K A Johnson and Paer Nordlund and Arne Holmgren and Heidi Erlandsen},
  journal={Proteins},
  year={2009},
  volume={74 1},
  pages={18-31}
}
YhaK is a protein of unknown function found in low abundance in the cytosol of Escherichia coli. DNA array studies have revealed that YhaK is strongly up-regulated by nitroso-glutathione (GSNO) and also displays a 12-fold increase in expression during biofilm growth of E. coli 83972 and VR50 in human urine. We have determined the YhaK crystal structure and demonstrated that in vitro YhaK is a good marker for monitoring oxidative stresses in E. coli. The YhaK protein structure shows a bicupin… CONTINUE READING