2arc: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|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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[[Category: Soisson, S M.]]
[[Category: Soisson, S M.]]
[[Category: Wolberger, C.]]
[[Category: Wolberger, C.]]
[[Category: ARA]]
[[Category: carbohydrate binding]]
[[Category: carbohydrate binding]]
[[Category: coiled-coil]]
[[Category: coiled-coil]]
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[[Category: transcription factor]]
[[Category: transcription factor]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:52:55 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:56:18 2008''

Revision as of 01:56, 31 March 2008

File:2arc.gif


PDB ID 2arc

Drag the structure with the mouse to rotate
, resolution 1.5Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE


OverviewOverview

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 StructureAbout this Structure

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

ReferenceReference

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

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