Thioester protein crosslinks

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[https://en.wikipedia.org/wiki/Thioester 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 ([https://en.wikipedia.org/wiki/Ubiquitin ubiquitinylation]). Thioester bonds in [https://en.wikipedia.org/wiki/Complement_system complement proteins] C3 and C4 are involved in tagging pathogens for destruction by the immune system, via the alternate complement activation pathway.
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[https://en.wikipedia.org/wiki/Thioester 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 ([https://en.wikipedia.org/wiki/Ubiquitin ubiquitinylation]). Thioester bonds in [https://en.wikipedia.org/wiki/Complement_system 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<ref name="slipknot">PMID: 30052296</ref>.
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==References==
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<references />

Revision as of 20:52, 23 June 2021

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). 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].

References

  1. ↑ Miller OK, Banfield MJ, Schwarz-Linek U. A new structural class of bacterial thioester domains reveals a slipknot topology. Protein Sci. 2018 Jul 27. doi: 10.1002/pro.3478. PMID:30052296 doi:http://dx.doi.org/10.1002/pro.3478

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Eric Martz

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