Crystal Structure of Invasin: A Bacterial Integrin-Binding Protein
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.
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The conformation of Als1 is similar to that of the pfam02368 family of bacterial immunoglobulin-like domain surface protein/adhesins, which includes the invasin of Y. pseudotuberculosis.
“The conformation of Als1 is similar to that of the pfam02368 family of bacterial immunoglobulin-like domain surface protein/adhesins, which includes the invasin of Y. pseudotuberculosis [42,43].”
From Als3 Is a Candida albicans Invasin That Binds to Cadherins and Induces Endocytosis by Host Cells (2007) · cites this paper as [43]
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References 57 · Cited by 287
- Authors
- Hamburger, Z. A., Brown, M. S., Isberg, R. R., & Bjorkman, P. J.
- Affiliations
- Division of Biology 156-29,
- Tufts University (US)
- ORCID
- Isberg, Ralph R.
- Venue
- Science
- Published
- 1999-10-08
- Volume
- 286
- Issue
- 5438
- Pages
- 291-295
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1980468009
- Cited by
- 287
- References
- 57
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 5 · 2023: 7 · 2022: 5 · 2021: 14 · 2020: 5 · 2019: 6 · 2018: 5 · 2017: 9 · 2016: 13 · 2015: 8 · 2014: 19 · 2013: 14 · 2012: 14
- FWCI
- 5.25
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- CaltechAUTHORS (California Institute of Technology) (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
- Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Yersinia bacterium, plague, ectoparasites research
- Keywords
- invasin, Yersinia pseudotuberculosis, integrin binding, fibronectin type III domain, convergent evolution, bacterial cell entry, extracellular domain structure, host-pathogen interaction
- MeSH terms
- Amino Acid Sequence, Bacterial Proteins, Binding Sites, Fibronectins, Hydrogen Bonding, Ligands, Models, Molecular, Protein Binding, Protein Conformation, Yersinia pseudotuberculosis, Integrins, Protein Structure, Secondary, Protein Folding, Crystallography, X-Ray, Adhesins, Bacterial, Evolution, Molecular
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