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2HZV

NikR-operator DNA complex

Summary for 2HZV
Entry DOI10.2210/pdb2hzv/pdb
Related1Q5V 1Q5Y 2HZA
Descriptor5'-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 Keywordsnickel, transcription factor, protein-dna complex, ribbon-helix-helix, metal binding protein-dna complex, metal binding protein/dna
Biological sourceEscherichia coli
Total number of polymer chains12
Total formula weight159482.33
Authors
Schreiter, E.R.,Drennan, C.L. (deposition date: 2006-08-09, release date: 2006-08-22, Last modification date: 2024-10-30)
Primary citationSchreiter, 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: 16945905
DOI: 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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건을2025-02-05부터공개중

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