Summary information and primary citation

PDB-id
1osl; SNAP-derived features in text and JSON formats; DNAproDB
Class
transcription-DNA
Method
NMR
Summary
Solution structure of a dimeric lactose DNA-binding domain complexed to a nonspecific DNA sequence
Reference
Kalodimos CG, Biris N, Bonvin AM, Levandoski MM, Guennuegues M, Boelens R, Kaptein R (2004): "Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes." Science, 305, 386-389. doi: 10.1126/science.1097064.
Abstract
Interaction of regulatory DNA binding proteins with their target sites is usually preceded by binding to nonspecific DNA. This speeds up the search for the target site by several orders of magnitude. We report the solution structure and dynamics of the complex of a dimeric lac repressor DNA binding domain with nonspecific DNA. The same set of residues can switch roles from a purely electrostatic interaction with the DNA backbone in the nonspecific complex to a highly specific binding mode with the base pairs of the cognate operator sequence. The protein-DNA interface of the nonspecific complex is flexible on biologically relevant time scales that may assist in the rapid and efficient finding of the target site.

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

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