From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1b9m.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1b9m.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1b9m| PDB=1b9m | SCENE= }} | | {{STRUCTURE_1b9m| PDB=1b9m | SCENE= }} |
| | | | |
| - | '''REGULATOR FROM ESCHERICHIA COLI'''
| + | ===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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_10075916}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10075916 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_10075916}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Ob fold]] | | [[Category: Ob fold]] |
| | [[Category: Winged helix turn helix]] | | [[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 Mon Jun 30 18:38:37 2008'' |
Revision as of 15:38, 30 June 2008
Template:STRUCTURE 1b9m
REGULATOR FROM ESCHERICHIA COLI
Template:ABSTRACT PUBMED 10075916
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 Mon Jun 30 18:38:37 2008
