Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein

Creators: Hamburger, Zsuzsa A.; Brown, Michele S.; Isberg, Ralph R.; Bjorkman, Pamela J.

Abstract

The Yersinia pseudotuberculosis invasin protein promotes bacterial entry by binding to host cell integrins with higher affinity than natural substrates such as fibronectin. The 2.3 angstrom crystal structure of the invasin extracellular region reveals five domains that form a 180 angstrom rod with structural similarities to tandem fibronectin type III domains. The integrin-binding surfaces of invasin and fibronectin include similarly located key residues, but in the context of different folds and surface shapes. The structures of invasin and fibronectin provide an example of convergent evolution, in which invasin presents an optimized surface for integrin binding, in comparison with host substrates.

Additional Information

© 1999 American Association for the Advancement of Science. Received 16 June 1999; accepted 1 September 1999. We thank S. M. Soltis and the staff at the Stanford Synchrotron Radiation Laboratory (SSRL) for help with xenon derivatization and data collection; M. J. Bennett, A. J. Chirino, L. M. Sánchez, D. E. Vaughn, and A. P. Yeh for discussions and help with crystallographic software; S. Matthews for intimin coordinates; P. D. Sun for CD94 coordinates; W. I. Weis for helpful discussions about C-type lectin structures; and W. I Weis, J. M. Leong, and members of the Bjorkman lab for critical reading of the manuscript. Inv497 coordinates have been deposited in the PDB (PDB code 1CWV).

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Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein

Abstract

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