Lysine-cysteine NOS bonds
From Proteopedia
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<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 chain, between Lys8 and Cys38, near the surface. | ||
{{Template:ColorKey_Amino2CarboxyRainbow}} | {{Template:ColorKey_Amino2CarboxyRainbow}} | ||
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| + | Oxidation breaks the NOS bond. In transaldolase, breaking the NOS bond causes subtle allosteric shifts in the catalytic site, decreasing enzymatic activity by several orders of magnitude<ref name="wensien2021" />. Thus, the NOS bond is described as an allosteric redox switch<ref name="wensien2021" />. | ||
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| + | A survey of the data in the [[Protein Data Bank]] revealed that the NOS bond likely exists "in diverse protein families across all domains of life (including ''Homo sapiens'') and that it is often located at catalytic or regulatory hotspots."<ref name="wensien2021" /> Because the NOS bond was unknown before 2021, it could easily have been overlooked in earlier interpretations of [[electron density maps]].<ref name="wensien2021" /> | ||
</StructureSection> | </StructureSection> | ||
Revision as of 23:49, 25 May 2021
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