Recognizing lysine-cysteine crosslinks in proteins

Article Multidisciplinary Sciences

A lysine-cysteine redox switch with an NOS bridge regulates enzyme function

Marie Wensien et al.

Summary: The discovery of a covalent crosslink between a cysteine and a lysine residue with a NOS bridge as an allosteric redox switch in the transaldolase enzyme of Neisseria gonorrhoeae is reported in this study. This redox switch leads to a structural relaxation mechanism that increases enzymatic activity in a significant way. The NOS bridge, found in diverse protein families across different organisms, can serve as a potential target for the development of new drugs and antibodies.

NATURE (2021)

Add to Collection

Editorial Material Multidisciplinary Sciences

Previously unknown type of protein crosslink discovered

Deborah Fass et al.

Summary: Molecular crosslinks like disulfides stabilize protein structures and regulate function, but a new type of regulatory protein crosslink involving a covalent linkage between cysteine and lysine residues has been discovered.

NATURE (2021)

Add to Collection

Article Multidisciplinary Sciences