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PDBsum entry 1dbq
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DNA-binding regulatory protein
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PDB id
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1dbq
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Mechanism of corepressor-Mediated specific DNA binding by the purine repressor.
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Authors
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M.A.Schumacher,
K.Y.Choi,
F.Lu,
H.Zalkin,
R.G.Brennan.
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Ref.
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Cell, 1995,
83,
147-155.
[DOI no: ]
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PubMed id
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Abstract
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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.
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