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==ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE==
==ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE==
<StructureSection load='2arc' size='340' side='right' caption='[[2arc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2arc' size='340' side='right'caption='[[2arc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2arc]] 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=2ARC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ARC FirstGlance]. <br>
<table><tr><td colspan='2'>[[2arc]] is a 2 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=2ARC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ARC FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARA:ALPHA-L-ARABINOSE'>ARA</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]] 1.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ara|2ara]], [[2aac|2aac]], [[1xja|1xja]], [[2k9s|2k9s]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARA:ALPHA-L-ARABINOSE'>ARA</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=2arc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2arc OCA], [http://pdbe.org/2arc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2arc RCSB], [http://www.ebi.ac.uk/pdbsum/2arc PDBsum]</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=2arc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2arc OCA], [https://pdbe.org/2arc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2arc RCSB], [https://www.ebi.ac.uk/pdbsum/2arc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2arc ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ARAC_ECOLI ARAC_ECOLI]] This protein controls the expression of at least six genes that are involved in the transport and catabolism of L-arabinose. It regulates initiation of transcription of the araBAD operon and it also controls its own synthesis. The L-arabinose operon displays both positive and negative regulation through AraC.  
[https://www.uniprot.org/uniprot/ARAC_ECOLI ARAC_ECOLI] This protein controls the expression of at least six genes that are involved in the transport and catabolism of L-arabinose. It regulates initiation of transcription of the araBAD operon and it also controls its own synthesis. The L-arabinose operon displays both positive and negative regulation through AraC.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ar/2arc_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ar/2arc_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 19: Line 20:
</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=2arc ConSurf].
</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=2arc ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of the arabinose-binding and dimerization domain of the Escherchia coli gene regulatory protein AraC was determined in the presence and absence of L-arabinose. The 1.5 angstrom structure of the arabinose-bound molecule shows that the protein adopts an unusual fold, binding sugar within a beta barrel and completely burying the arabinose with the amino-terminal arm of the protein. Dimer contacts in the presence of arabinose are mediated by an antiparallel coiled-coil. In the 2.8 angstrom structure of the uncomplexed protein, the amino-terminal arm is disordered, uncovering the sugar-binding pocket and allowing it to serve as an oligomerization interface. The ligand-gated oligomerization as seen in AraC provides the basis of a plausible mechanism for modulating the protein's DNA-looping properties.
Structural basis for ligand-regulated oligomerization of AraC.,Soisson SM, MacDougall-Shackleton B, Schleif R, Wolberger C Science. 1997 Apr 18;276(5311):421-5. PMID:9103202<ref>PMID:9103202</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
==See Also==
</div>
*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
<div class="pdbe-citations 2arc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Escherichia coli]]
[[Category: Soisson, S M]]
[[Category: Large Structures]]
[[Category: Wolberger, C]]
[[Category: Soisson SM]]
[[Category: Carbohydrate binding]]
[[Category: Wolberger C]]
[[Category: Coiled-coil]]
[[Category: Jelly roll]]
[[Category: Transcription factor]]

Latest revision as of 12:14, 14 February 2024

ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSEESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE

Structural highlights

2arc is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ARAC_ECOLI This protein controls the expression of at least six genes that are involved in the transport and catabolism of L-arabinose. It regulates initiation of transcription of the araBAD operon and it also controls its own synthesis. The L-arabinose operon displays both positive and negative regulation through AraC.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2arc, resolution 1.50Å

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