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Nat Struct Biol. 1999 May;6(5):427-32.

Structure of the arginine repressor from Bacillus stearothermophilus.

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  • 1Department of Biochemistry & Biophysics and Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.

Abstract

The arginine repressor (ArgR) is a hexameric DNA-binding protein that plays a multifunctional role in the bacterial cell. Here, we present the 2.5 A structure of apo-ArgR from Bacillus stearothermophilus and the 2.2 A structure of the hexameric ArgR oligomerization domain with bound arginine. This first view of intact ArgR reveals an approximately 32-symmetric hexamer of identical subunits, with six DNA-binding domains surrounding a central oligomeric core. The difference in quaternary organization of subunits in the arginine-bound and apo forms provides a possible explanation for poor operator binding by apo-ArgR and for high affinity binding in the presence of arginine.

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