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  • Title: NMR structure of the C-terminal domain of SecA in the free state.
    Author: Matousek WM, Alexandrescu AT.
    Journal: Biochim Biophys Acta; 2004 Nov 01; 1702(2):163-71. PubMed ID: 15488768.
    Abstract:
    SecA is an integral component of the prokaryotic Sec preprotein secretory translocase system. We report here the solution NMR structure of a fragment corresponding to the C-terminal domain of Escherichia coli SecA. In the presence of Zn2+, the fragment adopts a shortened version of the classic betabetaalpha zinc finger fold. The isolated C-terminal domain shows substantial differences from the X-ray structure of a homologous SecA domain bound to the chaperone-like cofactor SecB. The differences between the structures of the free and bound forms suggest that binding to SecB causes a perturbation of the C-terminal domain's intrinsically favored betabetaalpha fold.
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