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1tm6
From Proteopedia
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[[Image:1tm6.gif|left|200px]] | [[Image:1tm6.gif|left|200px]] | ||
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'''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA''' | '''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA''' | ||
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[[Category: Alexandrescu, A T.]] | [[Category: Alexandrescu, A T.]] | ||
[[Category: Matousek, W M.]] | [[Category: Matousek, W M.]] | ||
| - | [[Category: | + | [[Category: Beta hairpin]] |
| - | [[Category: | + | [[Category: Seca]] |
| - | [[Category: | + | [[Category: Zinc finger]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:07:20 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 07:07, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 10:07:20 2008
