1tm6 | pdb_00001tm6
NMR Structure of the Free Zinc Binding C-terminal Domain of SecA
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Overview
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.
About this Structure
1TM6 is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Full crystallographic information is available from OCA.
Reference
NMR structure of the C-terminal domain of SecA in the free state., Matousek WM, Alexandrescu AT, Biochim Biophys Acta. 2004 Nov 1;1702(2):163-71. PMID:15488768
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