1tm6: Difference between revisions

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[[Image:1tm6.gif|left|200px]]<br /><applet load="1tm6" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1tm6.gif|left|200px]]<br /><applet load="1tm6" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1tm6" />

'''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1TM6 OCA].

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==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Alexandrescu, A.T.]]

[[Category: Alexandrescu, A T.]]

[[Category: Matousek, W.M.]]

[[Category: Matousek, W M.]]

[[Category: ZN]]

[[Category: beta hairpin]]

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[[Category: zinc finger]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:03 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1tm6.gif|left|200px]]<br /><applet load="1tm6" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1tm6.gif|left|200px]]<br /><applet load="1tm6" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1tm6" />
 '''NMR Structure of the Free Zinc Binding C-terminal Domain of SecA'''<br />
 ==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.
+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==
-TM6 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TM6 OCA].
+TM6 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==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Alexandrescu, A.T.]]
+[[Category: Alexandrescu, A T.]]
-[[Category: Matousek, W.M.]]
+[[Category: Matousek, W M.]]
 [[Category: ZN]]
 [[Category: beta hairpin]]
@@ Line 20: / Line 20: @@
 [[Category: zinc finger]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:24:12 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:15:03 2008''