1ouz: Difference between revisions
New page: left|200px<br /><applet load="1ouz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ouz, resolution 2.41Å" /> '''Crystal structure of... |
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[[Image:1ouz.gif|left|200px]]<br /><applet load="1ouz" size=" | [[Image:1ouz.gif|left|200px]]<br /><applet load="1ouz" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ouz, resolution 2.41Å" /> | caption="1ouz, resolution 2.41Å" /> | ||
'''Crystal structure of a mutant IHF (BetaE44A) complexed with a variant H' Site (T44A)'''<br /> | '''Crystal structure of a mutant IHF (BetaE44A) complexed with a variant H' Site (T44A)'''<br /> | ||
==Overview== | ==Overview== | ||
Integration host factor (IHF) is a DNA-bending protein that recognizes its | 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== | ||
1OUZ 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:// | 1OUZ 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=1OUZ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Gardner, J | [[Category: Gardner, J F.]] | ||
[[Category: Lynch, T | [[Category: Lynch, T W.]] | ||
[[Category: Mattis, A | [[Category: Mattis, A N.]] | ||
[[Category: Read, E | [[Category: Read, E K.]] | ||
[[Category: Rice, P | [[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]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:21:51 2008'' | ||
Revision as of 12:21, 21 February 2008
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Crystal structure of a mutant IHF (BetaE44A) complexed with a variant 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
1OUZ 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
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