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Cited by 345

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Stabilizing Isopeptide Bonds Revealed in Gram-Positive Bacterial Pilus Structure

Open access
Kang, Hae Joo, Coulibaly, Fasséli, Clow, Fiona, Proft, Thomas, Baker, Edward N.·2007·Science

Abstract

Many bacterial pathogens have long, slender pili through which they adhere to host cells. The crystal structure of the major pilin subunit from the Gram-positive human pathogen Streptococcus pyogenes at 2.2 angstroms resolution reveals an extended structure comprising two all-β domains. The molecules associate in columns through the crystal, with each carboxyl terminus adjacent to a conserved lysine of the next molecule. This lysine forms the isopeptide bonds that link the subunits in native pili, validating the relevance of the crystal assembly. Each subunit contains two lysine-asparagine isopeptide bonds generated by an intramolecular reaction, and we find evidence for similar isopeptide bonds in other cell surface proteins of Gram-positive bacteria. The present structure explains the strength and stability of such Gram-positive pili and could facilitate vaccine development.

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Metadata

Authors
Kang, H. J., Coulibaly, F., Clow, F., Proft, T., & Baker, E. N.
Venue
Science
Published
2007-12-07
Volume
318
Issue
5856
Pages
1625-1628
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2056680298
Cited by
345
References
2
FWCI
8.02
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Stabilizing Isopeptide Bonds Revealed in Gram-Positive Bacterial Pilus Structure. https://app.cochat.ai/papers/10.1126/science.1145806
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Kang, H. J., Coulibaly, F., Clow, F., Proft, T., & Baker, E. N. (2007). Stabilizing Isopeptide Bonds Revealed in Gram-Positive Bacterial Pilus Structure. Science. https://doi.org/10.1126/science.1145806

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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