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Volume 593 Issue 7859, 20 May 2021

Joint venture

The amino acids that make up a protein dictate its structure and function. But crosslinks between amino-acid residues introduce additional chemical modifications that affect how the protein behaves under different physiological conditions. The most common links are between two sulfur atoms, known as disulfides. In this week’s issue, Kai Tittmann and his colleagues report a hitherto unidentified linkage that forms between cysteine and lysine residues, involving nitrogen and sulfur being joined together by an atom of oxygen (pictured on the cover with nitrogen in blue, oxygen in red and sulfur in yellow). The researchers found that this N–O–S bridge acts as a regulatory redox switch that controls the activity of the transaldolase enzyme in Neisseria gonorrhoeae, the bacterium that causes gonorrhoea. The team also did some research on structures in the Protein Data Bank and suggest that the N–O–S linkage is likely to be found in many other protein families.

Cover image: Kai Tittmann.

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