Thioester protein crosslinks: Difference between revisions
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<StructureSection load='' size='350' side='right' caption='' scene=''> | <StructureSection load='' size='350' side='right' caption='' scene=''> | ||
[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]; see also [[Ubiquitin and Ubiquitination]]). 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>. Many surface proteins of Gram-positive bacteria are predicted to contain TED as well as [[isopeptide bond|isopeptide]] and ester cross-links. This family of proteins is termed <b>TIE proteins</b> for thioester, isopeptide, ester proteins<ref name="slipknot" />. | [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]; see also [[Ubiquitin and Ubiquitination]]). 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>. Many surface proteins of Gram-positive bacteria are predicted to contain TED as well as [[isopeptide bond|isopeptide]] and ester cross-links. This family of proteins is termed <b>TIE proteins</b> for thioester, isopeptide, ester proteins<ref name="slipknot" />. | ||
</StructureSection> | </StructureSection> | ||
==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 00:17, 24 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; 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]. 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[1]. |
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ReferencesReferences
- ↑ 1.0 1.1 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