title: Solution structure of DnaE intein from Nostoc punctiforme: structural basis for the design of a new split intein suitable for site-specific chemical modification.
abstract: Naturally split DnaE intein from Nostoc punctiforme (Npu) has robust protein trans-splicing activity and high tolerance of sequence variations at the splicing junctions. We determined the solution structure of a single chain variant of NpuDnaE intein by NMR spectroscopy. Based on the NMR structure and the backbone dynamics of the single chain NpuDnaE intein, we designed a functional split variant of the NpuDnaE intein having a short C-terminal half (C-intein) composed of six residues. In vivo and in vitro protein ligation of model proteins by the newly designed split intein were demonstrated.
authors.affiliation: Research Program in Structural Biology and Biophysics, Institute of Biotechnology, University of Helsinki, P.O. Box 65, Helsinki FIN-00014, Finland.
authors.forename: Jesper S
authors.initials: JS
authors.lastname: Oeemig
authors.forename: A Sesilja
authors.initials: AS
authors.lastname: Aranko
authors.forename: Janica
authors.initials: J
authors.lastname: Djupsjöbacka
authors.forename: Kimmo
authors.initials: K
authors.lastname: Heinämäki
authors.forename: Hideo
authors.initials: H
authors.lastname: Iwaï