Thioether protein crosslinks

Thioether bonds between the sidechains of cysteine and tyrosine have been well studied in cysteine dioxygenases^[1].

Thioether bonds between cysteine and ligands are common, but are generally not crosslinks between polypeptides. Thioether bonds between cysteine and the vinyl groups of hemes are common. Diverse other ligands are bonded to protein via cysteine thioether linkages.

Note that the sidechain of methionine contains a thioether.

An accurate estimate of the frequency of thioether crosslinks in the PDB may not be available. A search for "thioether" in Proteopedia yields >200 hits in abstracts of pages titled with 4-character PDB codes.

ExamplesExamples

Cys-TyrCys-Tyr

1gof (1991): Galactose oxidase.
6e87 (2019): Cysteine dioxygenase.

Cys-LigandCys-Ligand

5nf0 (2017): Peptide cyclized via 2 thioethers with xylene.
6o83 (2019): Ubiquitin-activating enzyme E1 thioether-bonded to a modified deoxy adenosine.
6vdq (2021): Bacterial peroxygenase thioether-bonded to heme.

Other Protein CrosslinksOther Protein Crosslinks

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

ReferencesReferences

↑ Davies CG, Fellner M, Tchesnokov EP, Wilbanks SM, Jameson GN. The Cys-Tyr Crosslink of Cysteine Dioxygenase changes the Optimum pH of Reaction without Structural Change. Biochemistry. 2014 Nov 12. PMID:25390690 doi:http://dx.doi.org/10.1021/bi501277a

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

Eric Martz

[1] Davies CG, Fellner M, Tchesnokov EP, Wilbanks SM, Jameson GN. The Cys-Tyr Crosslink of Cysteine Dioxygenase changes the Optimum pH of Reaction without Structural Change. Biochemistry. 2014 Nov 12. PMID:25390690 doi:http://dx.doi.org/10.1021/bi501277a

[1]