1OSL
Solution structure of a dimeric lactose DNA-binding domain complexed to a nonspecific DNA sequence
Summary for 1OSL
| Entry DOI | 10.2210/pdb1osl/pdb |
| Related | 1L1M |
| NMR Information | BMRB: 5791 |
| Descriptor | 5'-D(*CP*GP*AP*TP*AP*AP*GP*AP*TP*AP*TP*CP*TP*TP*AP*TP*CP*G)-3', Lactose operon repressor (2 entities in total) |
| Functional Keywords | protein-dna complex, lac repressor, nonspecific interaction, transcription-dna complex, transcription/dna |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 24674.72 |
| Authors | Kalodimos, C.G.,Bonvin, A.M.J.J.,Boelens, R.,Kaptein, R. (deposition date: 2003-03-20, release date: 2004-05-04, Last modification date: 2021-10-27) |
| Primary citation | Kalodimos, C.G.,Biris, N.,Bonvin, A.M.,Levandoski, M.M.,Guennuegues, M.,Boelens, R.,Kaptein, R. Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes. Science, 305:386-389, 2004 Cited by PubMed 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. PubMed: 15256668DOI: 10.1126/science.1097064 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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