@article {46400,
	title = {Crystal structure of the nickel-responsive transcription factor NikR.},
	journal = {Nature Structural Biology},
	volume = {10},
	year = {2003},
	month = {2003 Oct},
	pages = {794-9},
	abstract = {<p>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.</p>
},
	keywords = {Amino Acid Sequence, Crystallography, X-Ray, Escherichia coli, Escherichia coli Proteins, Molecular Sequence Data, Nickel, Protein Structure, Tertiary, Repressor Proteins},
	issn = {1072-8368},
	doi = {10.1038/nsb985},
	author = {Schreiter, Eric R and Sintchak, Michael D and Guo, Yayi and Chivers, Peter T and Sauer, Robert T and Drennan, Catherine L}
}
