1b9n: Difference between revisions
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[[Image:1b9n.jpg|left|200px]] | [[Image:1b9n.jpg|left|200px]] | ||
'''REGULATOR FROM ESCHERICHIA COLI''' | {{Structure | ||
|PDB= 1b9n |SIZE=350|CAPTION= <scene name='initialview01'>1b9n</scene>, resolution 2.09Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''REGULATOR FROM ESCHERICHIA COLI''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1B9N is a [ | 1B9N 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=1B9N OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10075916 10075916] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: winged helix turn helix]] | [[Category: winged helix turn helix]] | ||
''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 10:08:09 2008'' | ||
Revision as of 11:08, 20 March 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. 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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