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1owg

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(New page: 200px<br /><applet load="1owg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1owg, resolution 2.10&Aring;" /> '''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"
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[[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==
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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.
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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==
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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].
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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==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Gardner, J.F.]]
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[[Category: Gardner, J F.]]
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[[Category: Lynch, T.W.]]
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[[Category: Lynch, T W.]]
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[[Category: Mattis, A.N.]]
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[[Category: Mattis, A N.]]
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[[Category: Read, E.K.]]
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[[Category: Read, E K.]]
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[[Category: Rice, P.A.]]
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[[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://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:14:59 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:22:21 2008''

Revision as of 12:22, 21 February 2008


1owg, resolution 2.10Å

Drag the structure with the mouse to rotate

Crystal structure of WT IHF complexed with an altered H' site (T44A)

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.

About this Structure

1OWG is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Integration host factor: putting a twist on protein-DNA recognition., Lynch TW, Read EK, Mattis AN, Gardner JF, Rice PA, J Mol Biol. 2003 Jul 11;330(3):493-502. PMID:12842466

Page seeded by OCA on Thu Feb 21 14:22:21 2008

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