Báo cáo khoa học: Stabilities and activities of the N- and C-domains of FKBP22 from a psychrotrophic bacterium overproduced in Escherichia coli

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FKBP22 from a psychrotrophic bacteriumShewanellasp. SIB1, is a dimer-ic protein with peptidyl prolyl cis-transisomerase (PPIase) activity. Accord-ing to homology modeling, it consists of an N-terminal domain, which is involved in dimerization of the protein, and a C-terminal catalytic domain. A longa3 helix spans these domains. An N-domain with the entirea3 helix (N-domain + ) and a C-domain with the entire a3 helix (C-domain + ) were overproduced inEscherichia coliin a His-tagged form, purified, and their biochemical properties were compared with those of the intact protein. C-domain + was shown to be a monomer and enzymatically active. Its opti-mum temperature for activity (10C) was identical to that of the intact protein. ...

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