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1o7l

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[[Image:1o7l.jpg|left|200px]]
 
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{{Structure
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==Molybdate-activated form of ModE from Escherichia coli==
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|PDB= 1o7l |SIZE=350|CAPTION= <scene name='initialview01'>1o7l</scene>, resolution 2.75&Aring;
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<StructureSection load='1o7l' size='340' side='right'caption='[[1o7l]], [[Resolution|resolution]] 2.75&Aring;' scene=''>
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|SITE= <scene name='pdbsite=MO1:Ca+Binding+Site+For+Chain+D'>MO1</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=MOO:MOLYBDATE ION'>MOO</scene>
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<table><tr><td colspan='2'>[[1o7l]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1O7L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1O7L FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.75&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MOO:MOLYBDATE+ION'>MOO</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1o7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o7l OCA], [https://pdbe.org/1o7l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1o7l RCSB], [https://www.ebi.ac.uk/pdbsum/1o7l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1o7l ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/o7/1o7l_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1o7l ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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ModE is a bacterial transcriptional regulator that orchestrates many aspects of molybdenum metabolism by binding to specific DNA sequences in a molybdate-dependent fashion. We present the crystal structure of Escherichia coli ModE in complex with molybdate, which was determined at 2.75A from a merohedrally twinned crystal (twin fraction approximately 0.30) with space group P4(3). We now have structures of ModE in both its "switched on" (ligand-bound) and "switched off" (apo) states. Comparison with the apo structure shows that ligand binding leads to extensive conformational changes not only in the molybdate-binding domain, but also in the DNA-binding domain. The most obvious difference is the loss of the pronounced asymmetry between the two chains of the ModE dimer, which had been a characteristic property of the apo structure. Another major change concerns the relative orientation of the two DNA-interacting winged helix-turn-helix motifs. Manual docking of an idealized DNA structure suggests that this conformational change should improve DNA binding of the activated molybdate-bound ModE.
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'''MOLYBDATE-ACTIVATED FORM OF MODE FROM ESCHERICHIA COLI'''
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Crystal structure of activated ModE reveals conformational changes involving both oxyanion and DNA-binding domains.,Schuttelkopf AW, Boxer DH, Hunter WN J Mol Biol. 2003 Feb 21;326(3):761-7. PMID:12581638<ref>PMID:12581638</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1o7l" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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ModE is a bacterial transcriptional regulator that orchestrates many aspects of molybdenum metabolism by binding to specific DNA sequences in a molybdate-dependent fashion. We present the crystal structure of Escherichia coli ModE in complex with molybdate, which was determined at 2.75A from a merohedrally twinned crystal (twin fraction approximately 0.30) with space group P4(3). We now have structures of ModE in both its "switched on" (ligand-bound) and "switched off" (apo) states. Comparison with the apo structure shows that ligand binding leads to extensive conformational changes not only in the molybdate-binding domain, but also in the DNA-binding domain. The most obvious difference is the loss of the pronounced asymmetry between the two chains of the ModE dimer, which had been a characteristic property of the apo structure. Another major change concerns the relative orientation of the two DNA-interacting winged helix-turn-helix motifs. Manual docking of an idealized DNA structure suggests that this conformational change should improve DNA binding of the activated molybdate-bound ModE.
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1O7L 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=1O7L OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of activated ModE reveals conformational changes involving both oxyanion and DNA-binding domains., Schuttelkopf AW, Boxer DH, Hunter WN, J Mol Biol. 2003 Feb 21;326(3):761-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12581638 12581638]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Hunter, W N.]]
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[[Category: Hunter WN]]
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[[Category: Schuttelkopf, A W.]]
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[[Category: Schuttelkopf AW]]
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[[Category: CA]]
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[[Category: CL]]
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[[Category: MOO]]
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[[Category: activator]]
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[[Category: dna binding]]
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[[Category: molybdate]]
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[[Category: mop]]
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[[Category: transcriptional regulator]]
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[[Category: winged helix-turn-helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:06:50 2008''
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Current revision

Molybdate-activated form of ModE from Escherichia coli

PDB ID 1o7l

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