Ester protein crosslinks

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Ester bonds between threonine and glutamine sidechains can form covalent cross-links between polypeptide chains[1]. First observed in repetitive domains of a putative surface-anchored adhesin of Clostridium perfringens (Gram positive)[1], analysis of sequences suggested "that these intramolecular ester bonds are a widespread and common feature of cell surface adhesion proteins in Gram-positive bacteria"[1].

Examples

  • 4ni6 REPEAT DOMAIN 1 OF CLOSTRIDIUM PERFRINGENS CPE0147
  • 4mkm REPEAT DOMAINS 1 & 2 OF CLOSTRIDIUM PERFRINGENS CPE0147

References

  1. ↑ 1.0 1.1 1.2 Kwon H, Squire CJ, Young PG, Baker EN. Autocatalytically generated Thr-Gln ester bond cross-links stabilize the repetitive Ig-domain shaft of a bacterial cell surface adhesin. Proc Natl Acad Sci U S A. 2013 Dec 16. PMID:24344302 doi:http://dx.doi.org/10.1073/pnas.1316855111

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