2ara

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{{STRUCTURE_2ara| PDB=2ara | SCENE= }}
{{STRUCTURE_2ara| PDB=2ara | SCENE= }}
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'''APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC'''
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===APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 9103202 is the PubMed ID number.
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{{ABSTRACT_PUBMED_9103202}}
==About this Structure==
==About this Structure==
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[[Category: Transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 19:22:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 04:21:16 2008''

Revision as of 01:21, 28 July 2008

Image:2ara.png

Template:STRUCTURE 2ara

APO FORM OF ESCHERICHIA COLI REGULATORY PROTEIN ARAC

Template:ABSTRACT PUBMED 9103202

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 Mon Jul 28 04:21:16 2008

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