2arc
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(New page: 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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Revision as of 06:11, 21 November 2007
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ESCHERICHIA COLI REGULATORY PROTEIN ARAC COMPLEXED WITH L-ARABINOSE
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
2ARC is a Single protein structure of sequence from Escherichia coli with ARA as ligand. 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 Wed Nov 21 08:18:59 2007
