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

@inproceedings{Callahan2011StructureOC,
  title={Structure of catalytically competent intein caught in a redox trap with functional and evolutionary implications},
  author={Brian P Callahan and Natalya I. Topilina and Matthew J. Stanger and Patrick Van Roey and Marlene Belfort},
  booktitle={Nature Structural &Molecular Biology},
  year={2011}
}
Here we describe self-splicing proteins, called inteins, that function as redox-responsive switches in bacteria. Redox regulation was achieved by engineering a disulfide bond between the intein's catalytic cysteine and a cysteine in the flanking 'extein' sequence. This interaction was validated by an X-ray structure, which includes a transient splice junction. A natural analog of the designed system was identified in Pyrococcus abyssi, suggesting an unprecedented form of adaptive, post… CONTINUE READING
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© 2 01 1 N at u re A m er ic a, In c. A ll ri g h ts r es

  • E Sabini
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  • 2000

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