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Crystal structure of WT IHF complexed with an altered H' site (T44A)Crystal structure of WT IHF complexed with an altered H' site (T44A)
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIntegration 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: 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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