Thioester protein crosslinks

Thioester bonds between cysteine and glutamine sidechains can form covalent cross-links between polypeptide chains.

• Thioester bonds are one way that ubiquitin may be attached to proteins (ubiquitinylation; see also Ubiquitin and Ubiquitination).

• Thioester bonds in complement proteins C3 and C4 are involved in tagging pathogens for destruction by the immune system, via the alternate complement activation pathway.

• Thioester bonds occur in thioester domains (TED) of Gram-positive bacteria, where they are thought to mediate covalent adhesion of bacteria to host cells^[1][2]. Many surface proteins of Gram-positive bacteria are predicted to contain TED as well as isopeptide and ester cross-links. This family of proteins is termed TIE proteins for thioester, isopeptide, ester proteins^[2]. Examples: 2xi9, 6fwy.
  • In a dramatic example, the pilus tip adhesin of Streptococcus pyogenes forms dimers in the presence of spermidine, a di-amine that forms thiopeptide bonds with the Gln211 residues in two adhesin protein chains^[3].