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<StructureSection load='3tb6' size='340' side='right'caption='[[3tb6]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
<StructureSection load='3tb6' size='340' side='right'caption='[[3tb6]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3tb6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"vibrio_subtilis"_ehrenberg_1835 "vibrio subtilis" ehrenberg 1835]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TB6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3tb6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TB6 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARB:BETA-L-ARABINOSE'>ARB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araC, araR, BSU33970, yvbS ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 "Vibrio subtilis" Ehrenberg 1835])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARB:BETA-L-ARABINOSE'>ARB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=3tb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb6 OCA], [https://pdbe.org/3tb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tb6 RCSB], [https://www.ebi.ac.uk/pdbsum/3tb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tb6 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=3tb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb6 OCA], [https://pdbe.org/3tb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tb6 RCSB], [https://www.ebi.ac.uk/pdbsum/3tb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tb6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/ARAR_BACSU ARAR_BACSU]] Transcriptional repressor of the arabinose utilization genes. Also regulates its own expression. Binds to two sequences within the promoters of the araABDLMNPQ-abfA operon and the araE gene, and to one sequence in the araR promoter.  
[https://www.uniprot.org/uniprot/ARAR_BACSU ARAR_BACSU] Transcriptional repressor of the arabinose utilization genes. Also regulates its own expression. Binds to two sequences within the promoters of the araABDLMNPQ-abfA operon and the araE gene, and to one sequence in the araR promoter.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Bacillus subtilis, the arabinose repressor AraR negatively controls the expression of genes in the metabolic pathway of arabinose-containing polysaccharides. The protein is composed of two domains of different phylogenetic origin and function: an N-terminal DNA-binding domain belonging to the GntR family and a C-terminal effector-binding domain that shows similarity to members of the GalR/LacI family. The crystal structure of the C-terminal effector-binding domain of AraR in complex with the effector L-arabinose has been determined at 2.2 A resolution. The L-arabinose binding affinity was characterized by isothermal titration calorimetry and differential scanning fluorimetry; the K(d) value was 8.4 +/- 0.4 microM. The effect of L-arabinose on the protein oligomeric state was investigated in solution and detailed analysis of the crystal identified a dimer organization which is distinctive from that of other members of the GalR/LacI family.
 
Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis.,Prochazkova K, Cermakova K, Pachl P, Sieglova I, Fabry M, Otwinowski Z, Rezacova P Acta Crystallogr D Biol Crystallogr. 2012 Feb;68(Pt 2):176-85. Epub 2012 Jan 17. PMID:22281747<ref>PMID:22281747</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3tb6" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Vibrio subtilis ehrenberg 1835]]
[[Category: Bacillus subtilis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Prochazkova, K]]
[[Category: Prochazkova K]]
[[Category: Rezacova, P]]
[[Category: Rezacova P]]
[[Category: Arabinose binding]]
[[Category: Dna binding protein]]
[[Category: Transcription regulation]]

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