Crystal Structure of an IHF-DNA Complex: A Protein-Induced DNA U-Turn

Phoebe A Rice; Shu-wei Yang; Kiyoshi Mizuuchi; Howard A. Nash

@article{Rice1996CrystalSO, title={Crystal Structure of an IHF-DNA Complex: A Protein-Induced DNA U-Turn}, author={Phoebe A Rice and Shu-wei Yang and Kiyoshi Mizuuchi and Howard A. Nash}, journal={Cell}, year={1996}, volume={87}, pages={1295-1306} }

Integration host factor (IHF) is a small heterodimeric protein that specifically binds to DNA and functions as an architectural factor in many cellular processes in prokaryotes. Here, we report the crystal structure of IHF complexed with 35 bp of DNA. The DNA is wrapped around the protein and bent by >160 degrees, thus reversing the direction of the helix axis within a very short distance. Much of the bending occurs at two large kinks where the base stacking is interrupted by intercalation of a… CONTINUE READING

F. M Richards
J . Mol . Biol .
1971

M. H. The Werner, A. M. Gronenborn, G. M. Clore
Science 271 , tions . Nature
1996

Crystal Structure of an IHF-DNA Complex: A Protein-Induced DNA U-Turn

From This Paper

Topics from this paper.

Explore Further: Topics Discussed in This Paper

Citations

Publications citing this paper.

Importance of the conserved TG/CA dinucleotide termini in phage Mu transposition: similarities to transposable elements in the human genome

The binding motif recognized by HU on both nicked and cruciform DNA.

Mapping the λ Integrase bridges in the nucleoprotein Holliday junction intermediates of viral integrative and excisive recombination.

Disruption and formation of surface salt bridges are coupled to DNA binding by the integration host factor: a computational analysis.

Refining the binding of Escherichia coli flagellar master regulator , FlhD 4 C 2 , on a base specific level

Variation of the intercalating proline in artificial peptides mimicking the DNA binding and bending IHF protein

Recombinational and transcriptional regulation within the class 1 integron

Structural and molecular dynamics simulation studies support Symplekin's protein scaffolding role and a novel fold in the TraI relaxase-helicase C-terminus is essential for conjugative DNA transfer

Pressure dissociation of integration host factor–DNA complexes reveals flexibility-dependent structural variation at the protein–DNA interface

Regulation of transcription from the fusion promoters generated by transposition of Tn4652 into the upstream region of pheBA operon in Pseudomonas putida

FILTER CITATIONS BY YEAR

CITATION STATISTICS

References

Publications referenced by this paper.

SQUASH - combining constraints for macromolecular phase refinement and extension.

The interaction of E. coli IHF protein with its specific binding sites

Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium.

Improved methods for building protein models in electron density maps and the location of errors in these models.

The interpretation of protein structure : estimation of static accessibility

Anatomy of a Flexer–DNA Complex inside a Higher-Order Transposition Intermediate

Examining the contribution of a dA+dT element to the conformation of Escherichia coli integration host factor-DNA complexes.

Intercala - structure of an oligo ( dA ) · oligo ( dT ) tract and its biological implication , DNA kinking , and the control of transcription

New parameters for the refinement of nucleic acid-containing structures.

The HU and IHF Proteins: Accessory Factors for Complex Protein-DNA Assemblies

Similar Papers