1OUZ

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

Summary for 1OUZ

• Entry DOI: 10.2210/pdb1ouz/pdb
• Related: 1IHF
• Descriptor: Phage lambda H' site, 5'-D(*GP*GP*CP*CP*AP*AP*AP*AP*AP*AP*GP*CP*AP*TP*T)-3', 5'-D(*GP*CP*TP*TP*AP*TP*CP*AP*AP*TP*TP*TP*GP*TP*AP*GP*CP*AP*CP*C)-3', ... (6 entities in total)
• Functional Keywords: protein-dna recognition, indirect readout, ihf, dna bending, transcription-dna complex, transcription/dna
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 43475.04

Authors

Lynch, T.W.,Read, E.K.,Mattis, A.N.,Gardner, J.F.,Rice, P.A. (deposition date: 2003-03-25, release date: 2003-07-15, Last modification date: 2023-08-16)

Primary citation

Lynch, T.W.,Read, E.K.,Mattis, A.N.,Gardner, J.F.,Rice, P.A.
Integration Host Factor: putting a twist on protein-DNA recognition
J.Mol.Biol., 330:493-502, 2003

PubMed 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.

PubMed: 12842466
DOI: 10.1016/S0022-2836(03)00529-1

Experimental method

X-RAY DIFFRACTION (2.41 Å)