Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications

An intein controlled by redox in bacteria is created by engineering a disulfide bond between the catalytic cysteine residue and the flanking polypeptide. A natural analog of this arrangement from Pyrococcus abyssi is found to respond to redox conditions in Escherichia coli, suggesting that inteins may function as biological sensors.

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