Ester protein crosslinks: Difference between revisions

← Older edit

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

Eric Martz

@@ 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" />.
+[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" /><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" />.
+==Examples==
+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.
+==Detection and Visualization==
+[[FirstGlance in Jmol]] alerts you to protein crosslinks when present, and provides convenient links that zoom in and and display each one in detail. Viewing the [[electron density map]] is just one more click. Use the links above to 4-character [[PDB codes]] to go to a Proteopedia page titled with that 4-character [[PDB code]]. There, click on "FirstGlance". In FirstGlance, click on the Tools tab, and there, on "Protein Crosslinks". See the practical guide [[FirstGlance/Evaluating Protein Crosslinks]].
+==Other Protein Crosslinks==
+In addition to the ester bonds discussed above, other [[Protein crosslinks|covalent cross-links between polypeptide chains]] include:
+*[[Disulfide bond]]s
+*[[Isopeptide bond]]s
+*[[Thioester protein crosslinks]]
+*[[Thioether protein crosslinks]]
+*[[Histidine-tyrosine protein crosslinks]]
+*[[Lysine-cysteine NOS bonds]]
+==See Also==
+*[[Esterification]]
 ==References==
 <references />