A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.

@article{Grosskinsky2007ACG,
  title={A conserved glycine residue of trimeric autotransporter domains plays a key role in Yersinia adhesin A autotransport.},
  author={Ulrike Grosskinsky and Monika Sch{\"u}tz and Michaela Fritz and Yvonne Schmid and Marina C. Lamparter and Pawel Szczesny and Andrei N. Lupas and I. Autenrieth and Dirk Linke},
  journal={Journal of bacteriology},
  year={2007},
  volume={189 24},
  pages={9011-9}
}
The Yersinia adhesin A (YadA) is a trimeric autotransporter adhesin of enteric yersiniae. It consists of three major domains: a head mediating adherence to host cells, a stalk involved in serum resistance, and an anchor that forms a membrane pore and is responsible for the autotransport function. The anchor contains a glycine residue, nearly invariant throughout trimeric autotransporter adhesins, that faces the pore lumen. To address the role of this glycine, we replaced it with polar amino… CONTINUE READING