Elongated fibrillar structure of a streptococcal adhesin assembled by the high-affinity association of alpha- and PPII-helices.

@article{Larson2010ElongatedFS,
  title={Elongated fibrillar structure of a streptococcal adhesin assembled by the high-affinity association of alpha- and PPII-helices.},
  author={Matthew R Larson and Kanagalaghatta R. Rajashankar and Manisha S. Patel and Rebekah A. Robinette and Paula J. Crowley and Suzanne M. Michalek and L. Jeannine Brady and Champion Deivanayagam},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 13},
  pages={5983-8}
}
Streptococcus mutans antigen I/II (AgI/II) is a cell surface-localized protein adhesin that interacts with salivary components within the salivary pellicle. AgI/II contributes to virulence and has been studied as an immunological and structural target, but a fundamental understanding of its underlying architecture has been lacking. Here we report a high-resolution (1.8 A) crystal structure of the A(3)VP(1) fragment of S. mutans AgI/II that demonstrates a unique fibrillar form (155 A) through… CONTINUE READING

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