1q5v
From Proteopedia
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'''Apo-NikR''' | '''Apo-NikR''' | ||
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[[Category: Schreiter, E R.]] | [[Category: Schreiter, E R.]] | ||
[[Category: Sintchak, M D.]] | [[Category: Sintchak, M D.]] | ||
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| - | [[Category: | + | [[Category: Ribbon-helix-helix domain]] |
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Revision as of 02:54, 3 May 2008
Apo-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
1Q5V is a Single protein structure of sequence from Escherichia coli. 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 Page seeded by OCA on Sat May 3 05:54:10 2008
