NikR is a ribbon-helix-helix DNA-binding protein

Citation
Pt. Chivers et Rt. Sauer, NikR is a ribbon-helix-helix DNA-binding protein, PROTEIN SCI, 8(11), 1999, pp. 2494-2500
Citations number
36
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN SCIENCE
ISSN journal
09618368 → ACNP
Volume
8
Issue
11
Year of publication
1999
Pages
2494 - 2500
Database
ISI
SICI code
0961-8368(199911)8:11<2494:NIARDP>2.0.ZU;2-#
Abstract
Escherichia coli NikR, a repressor with homologs in other bacteria and arch aea, was identified as a potential new member of the ribbon-helix-helix (be ta-alpha-alpha) family of transcription factors in profile based sequence s earches and in structure prediction experiments. Biophysical and biochemica l characterization of the N-terminal domain of NikR show that it has many f eatures expected of a beta-alpha-alpha protein including alpha-helical cont ent, dimeric solution form, concentration dependent thermal stability, and ability to bind DNA in sequence-specific manner. Mutation of a residue pred icted to be important for DNA-binding reduces operator affinity but does no t affect the secondary structure or stability of the protein.