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Science 18 April 1997:
Vol. 276. no. 5311, pp. 421 - 425
DOI: 10.1126/science.276.5311.421
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Reports

Structural Basis for Ligand-Regulated Oligomerization of AraC

Stephen M. Soisson, Beth MacDougall-Shackleton, Robert Schleif, * Cynthia Wolberger *

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.

S. M. Soisson, Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
B. MacDougall-Shackleton and R. Schleif, Biology Department, Johns Hopkins University, 3400 North Charles Street, Baltimore, MD 21218, USA.
C. Wolberger, Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
*   To whom correspondence should be addressed. E-mail: bob{at}gene.bio.jhu.edu (R.S) or cynthia{at}groucho.med.jhmi.edu (C.W.)

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