3tb6: Difference between revisions
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[[ | ==Structure of the effector-binding domain of arabinose repressor AraR from Bacillus subtilis== | ||
<StructureSection load='3tb6' size='340' side='right' caption='[[3tb6]], [[Resolution|resolution]] 2.21Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3tb6]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TB6 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARB:BETA-L-ARABINOSE'>ARB</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">araC, araR, BSU33970, yvbS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</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=3tb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tb6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tb6 RCSB], [http://www.ebi.ac.uk/pdbsum/3tb6 PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Prochazkova, K | [[Category: Prochazkova, K]] | ||
[[Category: Rezacova, P | [[Category: Rezacova, P]] | ||
[[Category: Arabinose binding]] | [[Category: Arabinose binding]] | ||
[[Category: Dna binding protein]] | [[Category: Dna binding protein]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
Revision as of 16:06, 9 December 2014
Structure of the effector-binding domain of arabinose repressor AraR from Bacillus subtilis
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