1owf
From Proteopedia
(New page: 200px<br /><applet load="1owf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1owf, resolution 1.95Å" /> '''Crystal structure of...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1owf.gif|left|200px]]<br /><applet load="1owf" size=" | + | [[Image:1owf.gif|left|200px]]<br /><applet load="1owf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1owf, resolution 1.95Å" /> | caption="1owf, resolution 1.95Å" /> | ||
'''Crystal structure of a mutant IHF (BetaE44A) complexed with the native H' Site'''<br /> | '''Crystal structure of a mutant IHF (BetaE44A) complexed with the native H' Site'''<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== | ||
| - | 1OWF 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:// | + | 1OWF 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=1OWF OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[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]] | ||
| Line 24: | Line 24: | ||
[[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 14:22:20 2008'' |
Revision as of 12:22, 21 February 2008
|
Crystal structure of a mutant IHF (BetaE44A) complexed with the native H' Site
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
1OWF 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 14:22:20 2008
