Summary information and primary citation

PDB-id
1owg; SNAP-derived features in text and JSON formats; DNAproDB
Class
transcription-DNA
Method
X-ray (2.1 Å)
Summary
Crystal structure of wt ihf complexed with an altered h' site (t44a)
Reference
Lynch TW, Read EK, Mattis AN, Gardner JF, Rice PA (2003): "Integration Host Factor: putting a twist on protein-DNA recognition." J.Mol.Biol., 330, 493-502. doi: 10.1016/S0022-2836(03)00529-1.
Abstract
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.

Cartoon-block schematics in six views (download the tarball)

PyMOL session file Download PDB file View in 3Dmol.js