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''' | + | {{Structure |
| + | |PDB= 1tm6 |SIZE=350|CAPTION= <scene name='initialview01'>1tm6</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TM6 is a [ | + | 1TM6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TM6 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15488768 15488768] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:20:14 2008'' |
Revision as of 12:20, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 14:20:14 2008
