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| | <StructureSection load='1b9m' size='340' side='right'caption='[[1b9m]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='1b9m' size='340' side='right'caption='[[1b9m]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1b9m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B9M FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1b9m]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B9M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B9M FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> |
| | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9m OCA], [http://pdbe.org/1b9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1b9m RCSB], [http://www.ebi.ac.uk/pdbsum/1b9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1b9m ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b9m OCA], [https://pdbe.org/1b9m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b9m RCSB], [https://www.ebi.ac.uk/pdbsum/1b9m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b9m ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MODE_ECOLI MODE_ECOLI]] The ModE-Mo complex acts as a repressor of the modABC operon, involved in the transport of molybdate. Upon binding molybdate, the conformation of the protein changes, promoting dimerization of ModE-Mo. The protein dimer is then competent to bind a DNA region, upstream of the modABC operon, which contains an 8-base inverted repeat 5'-TAACGTTA-3' flanked by two CAT boxes. Acts also as an enhancer of the expression of genes coding for molybdoenzymes, both directly and indirectly. ModE also interacts with tungstate. | + | [[https://www.uniprot.org/uniprot/MODE_ECOLI MODE_ECOLI]] The ModE-Mo complex acts as a repressor of the modABC operon, involved in the transport of molybdate. Upon binding molybdate, the conformation of the protein changes, promoting dimerization of ModE-Mo. The protein dimer is then competent to bind a DNA region, upstream of the modABC operon, which contains an 8-base inverted repeat 5'-TAACGTTA-3' flanked by two CAT boxes. Acts also as an enhancer of the expression of genes coding for molybdoenzymes, both directly and indirectly. ModE also interacts with tungstate. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1b9m" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1b9m" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| Structural highlights
Function
[MODE_ECOLI] The ModE-Mo complex acts as a repressor of the modABC operon, involved in the transport of molybdate. Upon binding molybdate, the conformation of the protein changes, promoting dimerization of ModE-Mo. The protein dimer is then competent to bind a DNA region, upstream of the modABC operon, which contains an 8-base inverted repeat 5'-TAACGTTA-3' flanked by two CAT boxes. Acts also as an enhancer of the expression of genes coding for molybdoenzymes, both directly and indirectly. ModE also interacts with tungstate.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Hall DR, Gourley DG, Leonard GA, Duke EM, Anderson LA, Boxer DH, Hunter WN. The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds. EMBO J. 1999 Mar 15;18(6):1435-46. PMID:10075916 doi:10.1093/emboj/18.6.1435
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