1tm6
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(New page: 200px<br /><applet load="1tm6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tm6" /> '''NMR Structure of the Free Zinc Binding C-ter...)
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Revision as of 01:16, 21 November 2007
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NMR Structure of the Free Zinc Binding C-terminal Domain of SecA
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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