2HZA

Nickel-bound full-length Escherichia coli NikR

Summary for 2HZA

• Entry DOI: 10.2210/pdb2hza/pdb
• Related: 1Q5V 1Q5Y 2HZV
• Descriptor: Nickel-responsive regulator, NICKEL (II) ION, 3-CYCLOHEXYLPROPYL 4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE, ... (4 entities in total)
• Functional Keywords: nickel-binding, ribbon-helix-helix, transcription factor, metal binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 31009.10

Authors

Schreiter, E.R.,Drennan, C.L. (deposition date: 2006-08-08, release date: 2006-08-22, Last modification date: 2024-11-20)

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

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

Experimental method

X-RAY DIFFRACTION (2.1 Å)