1ouz: Difference between revisions

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[[Image:1ouz.gif|left|200px]]
{{Seed}}
[[Image:1ouz.png|left|200px]]


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{{STRUCTURE_1ouz|  PDB=1ouz  |  SCENE=  }}  
{{STRUCTURE_1ouz|  PDB=1ouz  |  SCENE=  }}  


'''Crystal structure of a mutant IHF (BetaE44A) complexed with a variant H' Site (T44A)'''
===Crystal structure of a mutant IHF (BetaE44A) complexed with a variant H' Site (T44A)===




==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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{{ABSTRACT_PUBMED_12842466}}


==About this Structure==
==About this Structure==
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[[Category: Indirect readout]]
[[Category: Indirect readout]]
[[Category: Protein-dna recognition]]
[[Category: Protein-dna recognition]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:18:42 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:42:20 2008''

Revision as of 23:42, 28 July 2008

File:1ouz.png

Template:STRUCTURE 1ouz

Crystal structure of a mutant IHF (BetaE44A) complexed with a variant H' Site (T44A)

Template:ABSTRACT PUBMED 12842466

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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