1b9n: Difference between revisions
New page: left|200px<br /><applet load="1b9n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b9n, resolution 2.09Å" /> '''REGULATOR FROM ESCHE... |
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[[Image:1b9n.jpg|left|200px]]<br /><applet load="1b9n" size=" | [[Image:1b9n.jpg|left|200px]]<br /><applet load="1b9n" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1b9n, resolution 2.09Å" /> | caption="1b9n, resolution 2.09Å" /> | ||
'''REGULATOR FROM ESCHERICHIA COLI'''<br /> | '''REGULATOR FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
The molybdate-dependent transcriptional regulator (ModE) from Escherichia | 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== | ==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:// | 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== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gourley, D | [[Category: Gourley, D G.]] | ||
[[Category: Hall, D | [[Category: Hall, D R.]] | ||
[[Category: Hunter, W | [[Category: Hunter, W N.]] | ||
[[Category: NI]] | [[Category: NI]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
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[[Category: winged helix turn helix]] | [[Category: winged helix turn helix]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:01 2008'' | ||
Revision as of 12:53, 21 February 2008
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REGULATOR FROM ESCHERICHIA COLI
OverviewOverview
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 StructureAbout this Structure
1B9N is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds., Hall DR, Gourley DG, Leonard GA, Duke EM, Anderson LA, Boxer DH, Hunter WN, EMBO J. 1999 Mar 15;18(6):1435-46. PMID:10075916
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