Thioester protein crosslinks
From Proteopedia
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*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 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" />. Examples: [[2xi9]], [[6fwy]]. | + | *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="nakata2021">PMID:33633705</ref><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" />. Examples: [[2xi9]], [[6fwy]]. |
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Revision as of 19:45, 28 June 2021
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Other Protein Cross-Links
In addition to the thioester bonds discussed above, other covalent cross-links between polypeptide chains include:
References
- ↑ Nakata M, Kreikemeyer B. Genetics, Structure, and Function of Group A Streptococcal Pili. Front Microbiol. 2021 Feb 9;12:616508. doi: 10.3389/fmicb.2021.616508., eCollection 2021. PMID:33633705 doi:http://dx.doi.org/10.3389/fmicb.2021.616508
- ↑ 2.0 2.1 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
