This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1b4b
From Proteopedia
Revision as of 10:49, 3 October 2014 by OCA (Talk | contribs)
1b4b is a 3 chain structure with sequence from Geobacillus stearothermophilus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Ni J, Sakanyan V, Charlier D, Glansdorff N, Van Duyne GD. Structure of the arginine repressor from Bacillus stearothermophilus. Nat Struct Biol. 1999 May;6(5):427-32. PMID:10331868 doi:http://dx.doi.org/10.1038/8229
