2ara: Difference between revisions

Revision as of 17:30, 21 February 2008

APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC

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

2ARA 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

Page seeded by OCA on Thu Feb 21 16:30:22 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:2ara.gif|left|200px]]<br /><applet load="2ara" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2ara.gif|left|200px]]<br /><applet load="2ara" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2ara, resolution 2.8&Aring;" />
 '''APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC'''<br />
 ==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==
-ARA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ARA OCA].
+ARA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARA OCA].
 ==Reference==
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 [[Category: Escherichia coli]]
 [[Category: Single protein]]
-[[Category: Soisson, S.M.]]
+[[Category: Soisson, S M.]]
 [[Category: Wolberger, C.]]
 [[Category: carbohydrate binding]]
@@ Line 20: / Line 20: @@
 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:18:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:22 2008''