Ester protein crosslinks: Difference between revisions

Revision as of 22:08, 4 July 2021

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^[1]. First observed in 2013 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].

ExamplesExamples

Ser-C-terminus:

1gdq (2001): Ester catalytic intermediate trapped in trypsin.
1jl0 (2001): Ester catalytic intermediate trapped in mutant decarboxylase.
2pnl (2007): Protease VP4 of infectious pancreatic necrosis virus.
3p06 (2011): Protease VP4 of tellina virus 1.
4izk, 4izj (2013): Protease VP4 of yellowtail ascites virus.

Thr-Gln:

4ni6 (2013): Repeat domain 1 of Clostridium perfringens CPE0147 surface-anchored adhesin.
4mkm (2013): Repeat domains 1 & 2 of Clostridium perfringens CPE0147 surface-anchored adhesin.

Other Protein CrosslinksOther Protein Crosslinks

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

ReferencesReferences

↑ ^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?)Proteopedia Page Contributors and Editors (what is this?)

Eric Martz

[kwon2014-1] 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

[1]

@@ Line 1: / Line 1: @@
-[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" />.
+[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 crosslinks have also been observed between serine and the carboxy termini of proteases (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).
 ==Examples==