2HZV
NikR-operator DNA complex
Summary for 2HZV
Entry DOI | 10.2210/pdb2hzv/pdb |
Related | 1Q5V 1Q5Y 2HZA |
Descriptor | 5'-D(*AP*GP*TP*AP*TP*GP*AP*CP*GP*AP*AP*TP*AP*CP*TP*TP*AP*AP*AP*AP*TP*CP*GP*TP*CP*AP*TP*AP*CP*T)-3', 5'-D(*AP*GP*TP*AP*TP*GP*AP*CP*GP*AP*TP*TP*TP*TP*AP*AP*GP*TP*AP*TP*TP*CP*GP*TP*CP*AP*TP*AP*CP*T)-3', Nickel-responsive regulator, ... (5 entities in total) |
Functional Keywords | nickel, transcription factor, protein-dna complex, ribbon-helix-helix, metal binding protein-dna complex, metal binding protein/dna |
Biological source | Escherichia coli |
Total number of polymer chains | 12 |
Total formula weight | 159482.33 |
Authors | Schreiter, E.R.,Drennan, C.L. (deposition date: 2006-08-09, release date: 2006-08-22, Last modification date: 2024-10-30) |
Primary citation | Schreiter, E.R.,Wang, S.C.,Zamble, D.B.,Drennan, C.L. NikR-operator complex structure and the mechanism of repressor activation by metal ions. Proc.Natl.Acad.Sci.Usa, 103:13676-13681, 2006 Cited by PubMed Abstract: Metal ion homeostasis is critical to the survival of all cells. Regulation of nickel concentrations in Escherichia coli is mediated by the NikR repressor via nickel-induced transcriptional repression of the nickel ABC-type transporter, NikABCDE. Here, we report two crystal structures of nickel-activated E. coli NikR, the isolated repressor at 2.1 A resolution and in a complex with its operator DNA sequence from the nik promoter at 3.1 A resolution. Along with the previously published structure of apo-NikR, these structures allow us to evaluate functional proposals for how metal ions activate NikR, delineate the drastic conformational changes required for operator recognition, and describe the formation of a second metal-binding site in the presence of DNA. They also provide a rare set of structural views of a ligand-responsive transcription factor in the unbound, ligand-induced, and DNA-bound states, establishing a model system for the study of ligand-mediated effects on transcription factor function. PubMed: 16945905DOI: 10.1073/pnas.0606247103 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.1 Å) |
Structure validation
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