2arc

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[[Image:2arc.gif|left|200px]]
[[Image:2arc.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2arc |SIZE=350|CAPTION= <scene name='initialview01'>2arc</scene>, resolution 1.5&Aring;
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The line below this paragraph, containing "STRUCTURE_2arc", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=ARA:ALPHA-L-ARABINOSE'>ARA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_2arc| PDB=2arc | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2arc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2arc RCSB]</span>
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}}
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'''ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE'''
'''ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE'''
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[[Category: Soisson, S M.]]
[[Category: Soisson, S M.]]
[[Category: Wolberger, C.]]
[[Category: Wolberger, C.]]
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[[Category: carbohydrate binding]]
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[[Category: Carbohydrate binding]]
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[[Category: coiled-coil]]
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[[Category: Coiled-coil]]
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[[Category: jelly roll]]
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[[Category: Jelly roll]]
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[[Category: transcription factor]]
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[[Category: Transcription factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:22:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:56:18 2008''
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Revision as of 16:22, 3 May 2008

Template:STRUCTURE 2arc

ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE


Overview

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.

About this Structure

2ARC is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 19:22:51 2008

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