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1q5v

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[[Image:1q5v.jpg|left|200px]]
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{{STRUCTURE_1q5v| PDB=1q5v | SCENE= }}
{{STRUCTURE_1q5v| PDB=1q5v | SCENE= }}
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'''Apo-NikR'''
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===Apo-NikR===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 12970756 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12970756}}
==About this Structure==
==About this Structure==
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[[Category: Homotetramer]]
[[Category: Homotetramer]]
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Revision as of 09:40, 29 July 2008

Image:1q5v.png

Template:STRUCTURE 1q5v

Apo-NikR

Template:ABSTRACT PUBMED 12970756

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

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