Thioether protein crosslinks: Difference between revisions
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* [[6o83]] (2019): Ubiquitin-activating enzyme E1 thioether-bonded to a modified deoxy adenosine. | * [[6o83]] (2019): Ubiquitin-activating enzyme E1 thioether-bonded to a modified deoxy adenosine. | ||
* [[6vdq]] (2021): Bacterial peroxygenase thioether-bonded to heme. | * [[6vdq]] (2021): Bacterial peroxygenase thioether-bonded to heme. | ||
==Other Protein Crosslinks== | |||
In addition to the thioester bonds discussed above, other [[Protein crosslinks|covalent cross-links between polypeptide chains]] include: | |||
*[[Disulfide bond]]s | |||
*[[Isopeptide bond]]s | |||
*[[Ester protein crosslinks]] | |||
*[[Lysine-cysteine NOS bonds]] | |||
==References== | ==References== | ||
<references /> | <references /> | ||
Revision as of 00:36, 5 July 2021
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
- 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