This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2arc
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2arc' size='340' side='right'caption='[[2arc]], [[Resolution|resolution]] 1.50Å' scene=''> | <StructureSection load='2arc' size='340' side='right'caption='[[2arc]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2arc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> |
| - | <tr id=' | + | <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'>[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> | <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 == | ||
| - | + | [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]] | ||
| Line 20: | 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. | ||
| - | + | ==See Also== | |
| - | + | *[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]] | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | == | + | |
| - | + | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Soisson | + | [[Category: Soisson SM]] |
| - | [[Category: Wolberger | + | [[Category: Wolberger C]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE
| |||||||||||

