The structure of E. coli IgG-binding protein D suggests a general model for bending and binding in trimeric autotransporter adhesins.

@article{Leo2011TheSO,
  title={The structure of E. coli IgG-binding protein D suggests a general model for bending and binding in trimeric autotransporter adhesins.},
  author={Jack C Leo and Andrzej Lyskowski and Katarina Hattula and Marcus D Hartmann and Heinz J. Schwarz and Sarah J Butcher and Dirk Linke and Andrei N. Lupas and Adrian Goldman},
  journal={Structure},
  year={2011},
  volume={19 7},
  pages={
          1021-30
        }
}
The Escherichia coli Ig-binding (Eib) proteins are trimeric autotransporter adhesins (TAAs) and receptors for IgG Fc. We present the structure of a large fragment of the passenger domain of EibD, the first TAA structure to have both a YadA-like head domain and the entire coiled-coil stalk. The stalk begins as a right-handed superhelix, but switches handedness halfway down. An unexpected β-minidomain joins the two and inserts a ∼120° rotation such that there is no net twist between the beginning… CONTINUE READING
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