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The structure of the gyrA intein provides a view of its active site prior to the initial step of the protein splicing pathway. An intact leaving group at the N-terminal splice junction displays a highly strained cis geometry that is potentially critical for driving the isomerization of the scissile peptide bond, inducing subsequent cleavage.
The recently determined structures of ScrY and LamB porin, with and without bound ligands, have provided atomic-level details about the transit pathway of sugars through these channels and in turn revealed a novel transport mechanism.
The NMR structure of a copper-binding domain of the protein responsible for Menkes' syndrome demonstrates that the Cys-xx-Cys motif is used by prokaryotes and eukaryotes to deal with heavy metals.
