Issue 71, 2024

Functional implications of unusual NOS and SONOS covalent linkages found in proteins

Abstract

The tertiary and quaternary structures of many proteins are stabilized by strong covalent forces, of which disulfide bonds are the most well known. A new type of intramolecular and intermolecular covalent bond has been recently reported, consisting of the Lys and Cys side-chains linked by an oxygen atom (NOS). These post-translational modifications are widely distributed amongst proteins, and are formed under oxidative conditions. Similar linkages are observed during antibiotic biosynthesis, where hydroxylamine intermediates are tethered to the sulfur of enzyme active site Cys residues. These linkages open the way to understanding protein structure and function, give new insights into enzyme catalysis and natural product biosynthesis, and offer new strategies for drug design.

Graphical abstract: Functional implications of unusual NOS and SONOS covalent linkages found in proteins

Article information

Article type
Highlight
Submitted
28 jun 2024
Accepted
31 jul 2024
First published
02 aug 2024
This article is Open Access
Creative Commons BY license

Chem. Commun., 2024,60, 9463-9471

Functional implications of unusual NOS and SONOS covalent linkages found in proteins

M. D. Lloyd, K. S. Gregory and K. R. Acharya, Chem. Commun., 2024, 60, 9463 DOI: 10.1039/D4CC03191A

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