1b9m
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:1b9m.jpg|left|200px]] | [[Image:1b9m.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_1b9m", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | | | + | {{STRUCTURE_1b9m| PDB=1b9m | SCENE= }} |
| - | | | + | |
| - | + | ||
| - | }} | + | |
'''REGULATOR FROM ESCHERICHIA COLI''' | '''REGULATOR FROM ESCHERICHIA COLI''' | ||
| Line 28: | Line 25: | ||
[[Category: Hall, D R.]] | [[Category: Hall, D R.]] | ||
[[Category: Hunter, W N.]] | [[Category: Hunter, W N.]] | ||
| - | [[Category: | + | [[Category: Dna-binding]] |
| - | [[Category: | + | [[Category: Gene regulation]] |
| - | [[Category: | + | [[Category: Molybdate]] |
| - | [[Category: | + | [[Category: Ob fold]] |
| - | [[Category: | + | [[Category: Winged helix turn helix]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:14:54 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 08:14, 2 May 2008
REGULATOR FROM ESCHERICHIA COLI
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.
About this Structure
1B9M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
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:10075916 Page seeded by OCA on Fri May 2 11:14:54 2008
