1dbq

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|PDB= 1dbq |SIZE=350|CAPTION= <scene name='initialview01'>1dbq</scene>, resolution 2.2&Aring;
|PDB= 1dbq |SIZE=350|CAPTION= <scene name='initialview01'>1dbq</scene>, resolution 2.2&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dbq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbq OCA], [http://www.ebi.ac.uk/pdbsum/1dbq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dbq RCSB]</span>
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[[Category: Schumacher, M A.]]
[[Category: Schumacher, M A.]]
[[Category: Zalkin, H.]]
[[Category: Zalkin, H.]]
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[[Category: MG]]
 
[[Category: dna-binding regulatory protein]]
[[Category: dna-binding regulatory protein]]
[[Category: purine repressor]]
[[Category: purine repressor]]
[[Category: transcription regulation]]
[[Category: transcription regulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:35:59 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:38:27 2008''

Revision as of 16:38, 30 March 2008


PDB ID 1dbq

Drag the structure with the mouse to rotate
, resolution 2.2Å
Ligands:
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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. 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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