1pnr: Difference between revisions

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New page: left|200px<br /><applet load="1pnr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pnr, resolution 2.700Å" /> '''PURINE REPRESSOR-HY...
 
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[[Image:1pnr.jpg|left|200px]]<br /><applet load="1pnr" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1pnr.jpg|left|200px]]<br /><applet load="1pnr" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1pnr, resolution 2.700&Aring;" />
caption="1pnr, resolution 2.700&Aring;" />
'''PURINE REPRESSOR-HYPOXANTHINE-PURF-OPERATOR COMPLEX'''<br />
'''PURINE REPRESSOR-HYPOXANTHINE-PURF-OPERATOR COMPLEX'''<br />


==Overview==
==Overview==
The three-dimensional structure of a ternary complex of the purine, repressor, PurR, bound to both its corepressor, hypoxanthine, and the, 16-base pair purF operator site has been solved at 2.7 A resolution by, x-ray crystallography. The bipartite structure of PurR consists of an, amino-terminal DNA-binding domain and a larger carboxyl-terminal, corepressor binding and dimerization domain that is similar to that of the, bacterial periplasmic binding proteins. The DNA-binding domain contains a, helix-turn-helix motif that makes base-specific contacts in the major, groove of the DNA. Base contacts are also made by residues of, symmetry-related alpha helices, the "hinge" helices, which bind deeply in, the minor groove. Critical to hinge helix-minor groove binding is the, intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as, "leucine levers" to pry open the minor groove and kink the purF operator, by 45 degrees.
The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.


==About this Structure==
==About this Structure==
1PNR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with HPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PNR OCA].  
1PNR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=HPA:'>HPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNR OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brennan, R.G.]]
[[Category: Brennan, R G.]]
[[Category: Choi, K.Y.]]
[[Category: Choi, K Y.]]
[[Category: Schumacher, M.A.]]
[[Category: Schumacher, M A.]]
[[Category: Zalkin, H.]]
[[Category: Zalkin, H.]]
[[Category: HPA]]
[[Category: HPA]]
[[Category: protein-dna complex]]
[[Category: protein-dna complex]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:30:43 2008''

Revision as of 12:30, 21 February 2008

File:1pnr.jpg


1pnr, resolution 2.700Å

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PURINE REPRESSOR-HYPOXANTHINE-PURF-OPERATOR COMPLEX

Overview

The three-dimensional structure of a ternary complex of the purine repressor, PurR, bound to both its corepressor, hypoxanthine, and the 16-base pair purF operator site has been solved at 2.7 A resolution by x-ray crystallography. The bipartite structure of PurR consists of an amino-terminal DNA-binding domain and a larger carboxyl-terminal corepressor binding and dimerization domain that is similar to that of the bacterial periplasmic binding proteins. The DNA-binding domain contains a helix-turn-helix motif that makes base-specific contacts in the major groove of the DNA. Base contacts are also made by residues of symmetry-related alpha helices, the "hinge" helices, which bind deeply in the minor groove. Critical to hinge helix-minor groove binding is the intercalation of the side chains of Leu54 and its symmetry-related mate, Leu54', into the central CpG-base pair step. These residues thereby act as "leucine levers" to pry open the minor groove and kink the purF operator by 45 degrees.

About this Structure

1PNR is a Single protein structure of sequence from Escherichia coli with HPA as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of LacI member, PurR, bound to DNA: minor groove binding by alpha helices., Schumacher MA, Choi KY, Zalkin H, Brennan RG, Science. 1994 Nov 4;266(5186):763-70. PMID:7973627

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