The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.

@article{Xu2007ThePB,
  title={The periplasmic bacterial molecular chaperone SurA adapts its structure to bind peptides in different conformations to assert a sequence preference for aromatic residues.},
  author={Xiao-hua Xu and Shu-Ying Wang and Yao-Xiong Hu and David B. McKay},
  journal={Journal of molecular biology},
  year={2007},
  volume={373 2},
  pages={367-81}
}
The periplasmic molecular chaperone protein SurA facilitates correct folding and maturation of outer membrane proteins in Gram-negative bacteria. It preferentially binds peptides that have a high fraction of aromatic amino acids. Phage display selections, isothermal titration calorimetry and crystallographic structure determination have been used to elucidate the basis of the binding specificity. The peptide recognition is imparted by the first peptidyl-prolyl isomerase (PPIase) domain of SurA… CONTINUE READING

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