1b9n: Difference between revisions

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[[Image:1b9n.jpg|left|200px]]<br /><applet load="1b9n" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1b9n.jpg|left|200px]]<br /><applet load="1b9n" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1b9n, resolution 2.09Å" />

'''REGULATOR FROM ESCHERICHIA COLI'''<br />

==Overview==

The molybdate-dependent transcriptional regulator (ModE) from Escherichia, coli functions as a sensor of molybdate concentration and a regulator for, transcription of operons involved in the uptake and utilization of the, essential element, molybdenum. We have determined the structure of ModE, using multi-wavelength anomalous dispersion. Selenomethionyl and native, ModE models are refined to 1. 75 and 2.1 A, respectively and describe the, architecture and structural detail of a complete transcriptional, regulator. ModE is a homodimer and each subunit comprises N- and, C-terminal domains. The N-terminal domain carries a winged, helix-turn-helix motif for binding to DNA and is primarily responsible for, ModE dimerization. The C-terminal domain contains the molybdate-binding, site and residues implicated in binding the oxyanion are identified. This, domain is divided into sub-domains a and b which have similar folds, although the organization of secondary structure elements varies. The, sub-domain fold is related to the oligomer binding-fold and similar to, that of the subunits of several toxins which are involved in extensive, protein-protein interactions. This suggests a role for the C-terminal, domain in the formation of the ModE-protein-DNA complexes necessary to, regulate transcription. Modelling of ModE interacting with DNA suggests, that a large distortion of DNA is not necessary for complex formation.

The molybdate-dependent transcriptional regulator (ModE) from Escherichia coli functions as a sensor of molybdate concentration and a regulator for transcription of operons involved in the uptake and utilization of the essential element, molybdenum. We have determined the structure of ModE using multi-wavelength anomalous dispersion. Selenomethionyl and native ModE models are refined to 1. 75 and 2.1 A, respectively and describe the architecture and structural detail of a complete transcriptional regulator. ModE is a homodimer and each subunit comprises N- and C-terminal domains. The N-terminal domain carries a winged helix-turn-helix motif for binding to DNA and is primarily responsible for ModE dimerization. The C-terminal domain contains the molybdate-binding site and residues implicated in binding the oxyanion are identified. This domain is divided into sub-domains a and b which have similar folds, although the organization of secondary structure elements varies. The sub-domain fold is related to the oligomer binding-fold and similar to that of the subunits of several toxins which are involved in extensive protein-protein interactions. This suggests a role for the C-terminal domain in the formation of the ModE-protein-DNA complexes necessary to regulate transcription. Modelling of ModE interacting with DNA suggests that a large distortion of DNA is not necessary for complex formation.

==About this Structure==

1B9N 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 NI as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1B9N OCA].

1B9N 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=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9N OCA].

==Reference==

Line 13:

[[Category: Escherichia coli]]

[[Category: Single protein]]

[[Category: Gourley, D.G.]]

[[Category: Gourley, D G.]]

[[Category: Hall, D.R.]]

[[Category: Hall, D R.]]

[[Category: Hunter, W.N.]]

[[Category: Hunter, W N.]]

[[Category: NI]]

[[Category: dna-binding]]

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[[Category: winged helix turn helix]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:01 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1b9n.jpg|left|200px]]<br /><applet load="1b9n" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1b9n.jpg|left|200px]]<br /><applet load="1b9n" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1b9n, resolution 2.09&Aring;" />
 '''REGULATOR FROM ESCHERICHIA COLI'''<br />
 ==Overview==
-The molybdate-dependent transcriptional regulator (ModE) from Escherichia, coli functions as a sensor of molybdate concentration and a regulator for, transcription of operons involved in the uptake and utilization of the, essential element, molybdenum. We have determined the structure of ModE, using multi-wavelength anomalous dispersion. Selenomethionyl and native, ModE models are refined to 1. 75 and 2.1 A, respectively and describe the, architecture and structural detail of a complete transcriptional, regulator. ModE is a homodimer and each subunit comprises N- and, C-terminal domains. The N-terminal domain carries a winged, helix-turn-helix motif for binding to DNA and is primarily responsible for, ModE dimerization. The C-terminal domain contains the molybdate-binding, site and residues implicated in binding the oxyanion are identified. This, domain is divided into sub-domains a and b which have similar folds, although the organization of secondary structure elements varies. The, sub-domain fold is related to the oligomer binding-fold and similar to, that of the subunits of several toxins which are involved in extensive, protein-protein interactions. This suggests a role for the C-terminal, domain in the formation of the ModE-protein-DNA complexes necessary to, regulate transcription. Modelling of ModE interacting with DNA suggests, that a large distortion of DNA is not necessary for complex formation.
+The molybdate-dependent transcriptional regulator (ModE) from Escherichia coli functions as a sensor of molybdate concentration and a regulator for transcription of operons involved in the uptake and utilization of the essential element, molybdenum. We have determined the structure of ModE using multi-wavelength anomalous dispersion. Selenomethionyl and native ModE models are refined to 1. 75 and 2.1 A, respectively and describe the architecture and structural detail of a complete transcriptional regulator. ModE is a homodimer and each subunit comprises N- and C-terminal domains. The N-terminal domain carries a winged helix-turn-helix motif for binding to DNA and is primarily responsible for ModE dimerization. The C-terminal domain contains the molybdate-binding site and residues implicated in binding the oxyanion are identified. This domain is divided into sub-domains a and b which have similar folds, although the organization of secondary structure elements varies. The sub-domain fold is related to the oligomer binding-fold and similar to that of the subunits of several toxins which are involved in extensive protein-protein interactions. This suggests a role for the C-terminal domain in the formation of the ModE-protein-DNA complexes necessary to regulate transcription. Modelling of ModE interacting with DNA suggests that a large distortion of DNA is not necessary for complex formation.
 ==About this Structure==
-B9N 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 NI as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1B9N OCA].
+B9N 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=NI:'>NI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9N OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Gourley, D.G.]]
+[[Category: Gourley, D G.]]
-[[Category: Hall, D.R.]]
+[[Category: Hall, D R.]]
-[[Category: Hunter, W.N.]]
+[[Category: Hunter, W N.]]
 [[Category: NI]]
 [[Category: dna-binding]]
@@ Line 23: / Line 23: @@
 [[Category: winged helix turn helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:29:09 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:01 2008''