Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer.

@article{Lovering2008IdentificationOD,
  title={Identification of dynamic structural motifs involved in peptidoglycan glycosyltransfer.},
  author={Andrew L. Lovering and Liza H de Castro and Natalie C. J. Strynadka},
  journal={Journal of molecular biology},
  year={2008},
  volume={383 1},
  pages={167-77}
}
We have determined the structure of a new form of the bifunctional peptidoglycan glycosyltransferase (GT)/transpeptidase penicillin-binding protein 2 from the pathogen Staphylococcus aureus. We observe several previously unstructured regions of the GT substrate-binding pockets, including a pi-bulge in the outer helix that may be responsible for the conformational flexibility of active-site motifs required for transfer of product to the donor binding site during processive rounds of… CONTINUE READING