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Structural basis for proteintrans-splicing by a bacterial intein-like domain - protein ligation without nucleophilic side chains
2013
The FEBS Journal
Protein splicing in trans by split inteins has become a useful tool for protein engineering in vivo and in vitro. Inteins require Cys, Ser or Thr at the first residue of the C-terminal flanking sequence because a thiol or hydroxyl group in the side chains is a nucleophile indispensable for the transesterification step during protein splicing. Newly-identified distinct sequences with homology to the hedgehog/intein superfamily, called bacterial intein-like (BIL) domains, often do not have Cys,
doi:10.1111/febs.12307
pmid:23621571
fatcat:at4hx2dyafha5hnnjytkjyv35u