2arc: Difference between revisions

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New page: left|200px<br /><applet load="2arc" size="450" color="white" frame="true" align="right" spinBox="true" caption="2arc, resolution 1.5Å" /> '''ESCHERICHIA COLI REGU...
 
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[[Image:2arc.gif|left|200px]]<br /><applet load="2arc" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2arc.gif|left|200px]]<br /><applet load="2arc" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2arc, resolution 1.5&Aring;" />
caption="2arc, resolution 1.5&Aring;" />
'''ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE'''<br />
'''ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE'''<br />


==Overview==
==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.
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==
==About this Structure==
2ARC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ARA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ARC OCA].  
2ARC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ARA:'>ARA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARC OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Soisson, S.M.]]
[[Category: Soisson, S M.]]
[[Category: Wolberger, C.]]
[[Category: Wolberger, C.]]
[[Category: ARA]]
[[Category: ARA]]
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[[Category: transcription factor]]
[[Category: transcription factor]]


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Revision as of 17:30, 21 February 2008

File:2arc.gif


2arc, resolution 1.5Å

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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 with as ligand. 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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