1tm6
From Proteopedia
(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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| - | [[Image:1tm6.gif|left|200px]]<br /><applet load="1tm6" size=" | + | [[Image:1tm6.gif|left|200px]]<br /><applet load="1tm6" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA'''<br /> | '''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | SecA is an integral component of the prokaryotic Sec preprotein secretory | + | 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== | ==About this Structure== | ||
| - | 1TM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1TM6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TM6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Alexandrescu, A | + | [[Category: Alexandrescu, A T.]] |
| - | [[Category: Matousek, W | + | [[Category: Matousek, W M.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: beta hairpin]] | [[Category: beta hairpin]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:03 2008'' |
Revision as of 13:15, 21 February 2008
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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 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
Page seeded by OCA on Thu Feb 21 15:15:03 2008
