1b9n: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1b9n |SIZE=350|CAPTION= <scene name='initialview01'>1b9n</scene>, resolution 2.09Å | |PDB= 1b9n |SIZE=350|CAPTION= <scene name='initialview01'>1b9n</scene>, resolution 2.09Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=NI:NICKEL (II) ION'>NI</scene> | |LIGAND= <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b9n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9n OCA], [http://www.ebi.ac.uk/pdbsum/1b9n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b9n RCSB]</span> | |||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Hall, D R.]] | [[Category: Hall, D R.]] | ||
[[Category: Hunter, W N.]] | [[Category: Hunter, W N.]] | ||
[[Category: dna-binding]] | [[Category: dna-binding]] | ||
[[Category: gene regulation]] | [[Category: gene regulation]] | ||
| Line 32: | Line 34: | ||
[[Category: winged helix turn helix]] | [[Category: winged helix turn helix]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:56:33 2008'' | ||
Revision as of 18:56, 30 March 2008
| |||||||
| , resolution 2.09Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
Page seeded by OCA on Sun Mar 30 18:56:33 2008