Lysine-cysteine NOS bonds
From Proteopedia
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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 covalent linkage between polypeptide chains. | 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 covalent linkage between polypeptide chains. | ||
| - | <scene name='88/883792/6zx4_nos_whole_molecule/1'>The NOS bond is located</scene> near the N-terminus of the 352 amino acid chain, between Lys8 and Cys38, near the surface. | + | <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, between Lys8 and Cys38, near the surface. |
{{Template:ColorKey_Amino2CarboxyRainbow}} | {{Template:ColorKey_Amino2CarboxyRainbow}} | ||
Revision as of 23:53, 25 May 2021
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References
- ↑ 1.0 1.1 1.2 1.3 1.4 Wensien M, von Pappenheim FR, Funk LM, Kloskowski P, Curth U, Diederichsen U, Uranga J, Ye J, Fang P, Pan KT, Urlaub H, Mata RA, Sautner V, Tittmann K. A lysine-cysteine redox switch with an NOS bridge regulates enzyme function. Nature. 2021 May 5. pii: 10.1038/s41586-021-03513-3. doi:, 10.1038/s41586-021-03513-3. PMID:33953398 doi:http://dx.doi.org/10.1038/s41586-021-03513-3
