Lysine-cysteine NOS bonds: Difference between revisions

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Eric Martz, Michal Harel

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 <StructureSection size='350' side='right' caption='' scene='88/883792/6zx4_nos/2'>
-Covalent Lysine-Cysteine protein crosslinks were first reported in 2016, interpreted at the time as Lys-CH<sub>2</sub>-Cys<ref name="methylene">PMID: 27261771</ref><ref name="matthews">PMID: 34180568</ref>. Lysine-cysteine "Nitrogen-Oxygen-Sulfur" (NOS) bonds (<scene name='88/883792/6zx4_nos/2'>restore initial scene</scene>) were first reported in 2021 in transaldolases<ref name="wensien2021">PMID: 33953398</ref>. The sidechains of a lysine and a cysteine, joined by an NOS bond, make a covalent linkage between polypeptide chains. For comparison, the [[disulfide bond]] is a far more common type of [[Protein crosslinks|covalent linkage between polypeptide chains]], and the [[isopeptide bond]] is another rare type.
+Covalent Lysine-Cysteine protein crosslinks were first reported in 2016, interpreted at the time as Lys-CH<sub>2</sub>-Cys<ref name="methylene">PMID: 27261771</ref><ref name="matthews">PMID: 34180568</ref>. In 2019, Jimin Wang provided evidence for oxygen rather than methylene as the linker<ref name="jimin">PMID: 30592103</ref>.
+Lysine-cysteine "Nitrogen-Oxygen-Sulfur" (NOS) bonds (<scene name='88/883792/6zx4_nos/2'>restore initial scene</scene>) were first reported in 2021 in transaldolases<ref name="wensien2021">PMID: 33953398</ref>. The sidechains of a lysine and a cysteine, joined by an NOS bond, make a covalent linkage between polypeptide chains. For comparison, the [[disulfide bond]] is a far more common type of [[Protein crosslinks|covalent linkage between polypeptide chains]], and the [[isopeptide bond]] is another rare type.
 <scene name='88/883792/6zx4_nos_whole_molecule/1'>The NOS bond is located</scene> near the N-terminus of the 352 amino acid ''Neisseria gonorrhoeae'' transaldolase chain [[6zx4]], between Lys8 and Cys38, near the surface.