Ester protein crosslinks

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[https://en.wikipedia.org/wiki/Ester Ester bonds] between threonine and glutamine sidechains can form covalent cross-links between polypeptide chains<ref name="kwon2014">PMID: 24344302</ref>. First observed in repetitive domains of a putative surface-anchored adhesin of ''Clostridium perfringens'' (Gram positive)<ref name="kwon2014" />, analysis of sequences suggested "that these intramolecular ester bonds are a widespread and common feature of cell surface adhesion proteins in Gram-positive bacteria"<ref name="kwon2014" />. In the examples studied, the Thr-Gln ester bonds occur between the first and last beta strands, increasing thermal stability and resisance to proteases<ref name="kwon2014" />. The structures containing such ester crosslinks "have in common is that they are very long and thin but also subject to large mechanical shear stresses and protease-rich environments"<ref name="kwon2014" />.
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[https://en.wikipedia.org/wiki/Ester Ester bonds] between threonine and glutamine sidechains can form covalent cross-links between polypeptide chains<ref name="kwon2014">PMID: 24344302</ref>. First observed in repetitive domains of a putative surface-anchored adhesin of ''Clostridium perfringens'' (Gram positive)<ref name="kwon2014" />, analysis of sequences suggested "that these intramolecular ester bonds are a widespread and common feature of cell surface adhesion proteins in Gram-positive bacteria"<ref name="kwon2014" />. In the examples studied, the Thr-Gln ester bonds occur between the first and last beta strands of immunoglobulin-like domains, increasing thermal stability and resisance to proteases<ref name="kwon2014" />. The structures containing such ester crosslinks "have in common is that they are very long and thin but also subject to large mechanical shear stresses and protease-rich environments"<ref name="kwon2014" />.
==Examples==
==Examples==

Revision as of 23:51, 30 June 2021

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]. In the examples studied, the Thr-Gln ester bonds occur between the first and last beta strands of immunoglobulin-like domains, increasing thermal stability and resisance to proteases[1]. The structures containing such ester crosslinks "have in common is that they are very long and thin but also subject to large mechanical shear stresses and protease-rich environments"[1].

Examples

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

Other Protein Crosslinks

In addition to the Ester crosslinks discussed above, other covalent cross-links between polypeptide chains include:

References

  1. ↑ 1.0 1.1 1.2 1.3 1.4 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

Proteopedia Page Contributors and Editors (what is this?)

Eric Martz

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