1DBQ

DNA-BINDING REGULATORY PROTEIN

Summary for 1DBQ

• Entry DOI: 10.2210/pdb1dbq/pdb
• Descriptor: PURINE REPRESSOR, MAGNESIUM ION (3 entities in total)
• Functional Keywords: transcription regulation, dna-binding regulatory protein, purine repressor
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 65053.42

Authors

Schumacher, M.A.,Choi, K.Y.,Lu, F.,Zalkin, H.,Brennan, R.G. (deposition date: 1996-02-13, release date: 1996-12-07, Last modification date: 2024-02-07)

Primary citation

Schumacher, M.A.,Choi, K.Y.,Lu, F.,Zalkin, H.,Brennan, R.G.
Mechanism of corepressor-mediated specific DNA binding by the purine repressor.
Cell(Cambridge,Mass.), 83:147-155, 1995

PubMed Abstract: 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.

PubMed: 7553867
DOI: 10.1016/0092-8674(95)90243-0

Experimental method

X-RAY DIFFRACTION (2.2 Å)