Ester protein crosslinks: Difference between revisions
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[https://en.wikipedia.org/wiki/Ester Ester] crosslinks between '''serine and the carboxy termini''' of proteases have been observed beginning in 2001 (see examples below). These are formed autocatalytically. Similar ester crosslinks exist in proteases in which ester intermediates in the catalytic process have been trapped (see examples below). | [https://en.wikipedia.org/wiki/Ester Ester] crosslinks between '''serine and the carboxy termini''' of proteases have been observed beginning in 2001 (see examples below). These are formed autocatalytically. Similar ester crosslinks exist in proteases in which ester intermediates in the catalytic process have been trapped (see examples below). | ||
Ester bonds between '''threonine and glutamine sidechains''' can also form covalent crosslinks between polypeptide chains<ref name="kwon2014">PMID: 24344302</ref>. First observed in 2013 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" />. | Ester bonds between '''threonine and glutamine sidechains''' can also form covalent crosslinks between polypeptide chains<ref name="kwon2014">PMID: 24344302</ref>. First observed in 2013 in repetitive domains of a putative surface-anchored adhesin of ''Clostridium perfringens'' (Gram positive)<ref name="kwon2014" /><ref name="baker2015">PMID: 26517883</ref>, 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" />. | ||