1Q5V

Apo-NikR

Summary for 1Q5V

• Entry DOI: 10.2210/pdb1q5v/pdb
• Related: 1Q5Y
• Descriptor: Nickel responsive regulator (2 entities in total)
• Functional Keywords: homotetramer, ribbon-helix-helix domain, beta sandwich, transcription
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 60475.22

Authors

Schreiter, E.R.,Sintchak, M.D.,Guo, Y.,Chivers, P.T.,Sauer, R.T.,Drennan, C.L. (deposition date: 2003-08-11, release date: 2003-09-30, Last modification date: 2024-02-14)

Primary citation

Schreiter, E.R.,Sintchak, M.D.,Guo, Y.,Chivers, P.T.,Sauer, R.T.,Drennan, C.L.
Crystal Structure of the Nickel-Responsive Transcription Factor NikR
Nat.Struct.Biol., 10:794-799, 2003

PubMed Abstract: NikR is a metal-responsive transcription factor that controls nickel uptake in Escherichia coli by regulating expression of a nickel-specific ATP-binding cassette (ABC) transporter. We have determined the first two structures of NikR: the full-length apo repressor at a resolution of 2.3 A and the nickel-bound C-terminal regulatory domain at a resolution of 1.4 A. NikR is the only known metal-responsive member of the ribbon-helix-helix family of transcription factors, and its structure has a quaternary arrangement consisting of two dimeric DNA-binding domains separated by a tetrameric regulatory domain that binds nickel. The position of the C-terminal regulatory domain enforces a large spacing between the contacts that each NikR DNA-binding domain can make with the nik operator. The regulatory domain of NikR contains four nickel-binding sites at the tetramer interface, each exhibiting a novel square-planar coordination by three histidines and one cysteine side chain.

PubMed: 12970756
DOI: 10.1038/nsb985

Experimental method

X-RAY DIFFRACTION (2.3 Å)