1q5y
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(New page: 200px<br /><applet load="1q5y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q5y, resolution 1.40Å" /> '''Nickel-Bound C-termi...)
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Revision as of 22:17, 20 November 2007
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Nickel-Bound C-terminal Regulatory Domain of NikR
Overview
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.
About this Structure
1Q5Y is a Single protein structure of sequence from Escherichia coli with NI and EDO as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the nickel-responsive transcription factor NikR., Schreiter ER, Sintchak MD, Guo Y, Chivers PT, Sauer RT, Drennan CL, Nat Struct Biol. 2003 Oct;10(10):794-9. Epub 2003 Sep 14. PMID:12970756
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