1owg: Difference between revisions

New page: left|200px<br /><applet load="1owg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1owg, resolution 2.10Å" /> '''Crystal structure of...
 
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[[Image:1owg.gif|left|200px]]<br /><applet load="1owg" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1owg.gif|left|200px]]<br /><applet load="1owg" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1owg, resolution 2.10&Aring;" />
caption="1owg, resolution 2.10&Aring;" />
'''Crystal structure of WT IHF complexed with an altered H' site (T44A)'''<br />
'''Crystal structure of WT IHF complexed with an altered H' site (T44A)'''<br />


==Overview==
==Overview==
Integration host factor (IHF) is a DNA-bending protein that recognizes its, cognate sites through indirect readout. Previous studies have shown that, binding of wild-type (WT)-IHF is disrupted by a T to A mutation at the, center position of a conserved TTR motif in its binding site, and that, substitution of betaGlu44 with Ala prevented IHF from discriminating, between A and T at this position. We have determined the crystal, structures and relative binding affinities for all combinations of WT-IHF, and IHF-betaGlu44Ala bound to the WT and mutant DNAs. Comparison of these, structures reveals that DNA twist plays a major role in DNA recognition by, IHF, and that this geometric parameter is dependent on the dinucleotide, step and not on the bound IHF variant.
Integration host factor (IHF) is a DNA-bending protein that recognizes its cognate sites through indirect readout. Previous studies have shown that binding of wild-type (WT)-IHF is disrupted by a T to A mutation at the center position of a conserved TTR motif in its binding site, and that substitution of betaGlu44 with Ala prevented IHF from discriminating between A and T at this position. We have determined the crystal structures and relative binding affinities for all combinations of WT-IHF and IHF-betaGlu44Ala bound to the WT and mutant DNAs. Comparison of these structures reveals that DNA twist plays a major role in DNA recognition by IHF, and that this geometric parameter is dependent on the dinucleotide step and not on the bound IHF variant.


==About this Structure==
==About this Structure==
1OWG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OWG OCA].  
1OWG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OWG OCA].  


==Reference==
==Reference==
Line 13: Line 13:
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Gardner, J.F.]]
[[Category: Gardner, J F.]]
[[Category: Lynch, T.W.]]
[[Category: Lynch, T W.]]
[[Category: Mattis, A.N.]]
[[Category: Mattis, A N.]]
[[Category: Read, E.K.]]
[[Category: Read, E K.]]
[[Category: Rice, P.A.]]
[[Category: Rice, P A.]]
[[Category: dna bending]]
[[Category: dna bending]]
[[Category: ihf]]
[[Category: ihf]]
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[[Category: protein-dna recognition]]
[[Category: protein-dna recognition]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:21 2008''

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