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2ara
From Proteopedia
(New page: 200px<br /><applet load="2ara" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ara, resolution 2.8Å" /> '''APO FORM OF ESCHERICH...) |
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| - | [[Image:2ara.gif|left|200px]]<br /><applet load="2ara" size=" | + | [[Image:2ara.gif|left|200px]]<br /><applet load="2ara" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2ara, resolution 2.8Å" /> | caption="2ara, resolution 2.8Å" /> | ||
'''APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC'''<br /> | '''APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the arabinose-binding and dimerization domain of | + | 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== | ||
| - | 2ARA 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:// | + | 2ARA 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== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Soisson, S | + | [[Category: Soisson, S M.]] |
[[Category: Wolberger, C.]] | [[Category: Wolberger, C.]] | ||
[[Category: carbohydrate binding]] | [[Category: carbohydrate binding]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:30:22 2008'' |
Revision as of 14:30, 21 February 2008
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APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC
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
2ARA 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 Thu Feb 21 16:30:22 2008
