| Literature DB >> 10595554 |
Abstract
Escherichia coli NikR, a repressor with homologs in other bacteria and archaea, was identified as a potential new member of the ribbon-helix-helix (beta-alpha-alpha) family of transcription factors in profile based sequence searches and in structure prediction experiments. Biophysical and biochemical characterization of the N-terminal domain of NikR show that it has many features expected of a beta-alpha-alpha protein including alpha-helical content, dimeric solution form, concentration dependent thermal stability, and ability to bind DNA in sequence-specific manner. Mutation of a residue predicted to be important for DNA-binding reduces operator affinity but does not affect the secondary structure or stability of the protein.Entities:
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Year: 1999 PMID: 10595554 PMCID: PMC2144182 DOI: 10.1110/ps.8.11.2494
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725