1b4b
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(New page: 200px<br /><applet load="1b4b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1b4b, resolution 2.2Å" /> '''STRUCTURE OF THE OLIG...)
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Revision as of 09:13, 20 November 2007
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STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF THE ARGININE REPRESSOR FROM BACILLUS STEAROTHERMOPHILUS
Overview
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.
About this Structure
1B4B is a Single protein structure of sequence from Geobacillus stearothermophilus with ARG as ligand. Full crystallographic information is available from OCA.
Reference
Structure of the arginine repressor from Bacillus stearothermophilus., Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD, Nat Struct Biol. 1999 May;6(5):427-32. PMID:10331868
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