1dbq
From Proteopedia
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DNA-BINDING REGULATORY PROTEIN
Overview
The modulation of the affinity of DNA-binding proteins by small molecule, effectors for cognate DNA sites is common to both prokaryotes and, eukaryotes. However, the mechanisms by which effector binding to one, domain affects DNA binding by a distal domain are poorly understood, structurally. In initial studies to provide insight into the mechanism of, effector-modulated DNA binding of the lactose repressor family, we, determined the crystal structure of the purine repressor bound to a, corepressor and purF operator. To extend our understanding, we have, determined the structure of the corepressor-free corepressor-binding, domain of the purine repressor at 2.2 A resolution. In the unliganded, state, structural changes in the corepressor-binding pocket cause each, subunit to rotate open by as much as 23 degrees, the consequences of which, are the disengagement of the minor groove-binding hinge helices and, repressor-DNA dissociation.
About this Structure
1DBQ is a Single protein structure of sequence from Escherichia coli with MG as ligand. Full crystallographic information is available from OCA.
Reference
Mechanism of corepressor-mediated specific DNA binding by the purine repressor., Schumacher MA, Choi KY, Lu F, Zalkin H, Brennan RG, Cell. 1995 Oct 6;83(1):147-55. PMID:7553867
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