The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll.

@article{Nummelin2004TheYA,
  title={The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll.},
  author={Heli Nummelin and Michael C. Merckel and Jack C Leo and Hilkka Lankinen and Mikael Skurnik and Adrian Goldman},
  journal={The EMBO journal},
  year={2004},
  volume={23 4},
  pages={
          701-11
        }
}
The crystal structure of the recombinant collagen-binding domain of Yersinia adhesin YadA from Yersinia enterocolitica serotype O:3 was solved at 1.55 A resolution. The trimeric structure is composed of head and neck regions, and the collagen binding head region is a novel nine-coiled left-handed parallel beta-roll. Before the beta-roll, the polypeptide loops from one monomer to the rest, and after the beta-roll the neck region does the same, making the transition from the globular head region… CONTINUE READING
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