@article {46404,
	title = {Ribbon-helix-helix transcription factors: variations on a theme.},
	journal = {Nature Reviews Microbiology},
	volume = {5},
	year = {2007},
	month = {2007 Sep},
	pages = {710-20},
	abstract = {<p>The ribbon-helix-helix (RHH) superfamily of transcription factors uses a conserved three-dimensional structural motif to bind to DNA in a sequence-specific manner. This functionally diverse protein superfamily regulates the transcription of genes that are involved in the uptake of metals, amino-acid biosynthesis, cell division, the control of plasmid copy number, the lytic cycle of bacteriophages and, perhaps, many other cellular processes. In this Analysis, the structures of different RHH transcription factors are compared in order to evaluate the sequence motifs that are required for RHH-domain folding and DNA binding, as well as to identify conserved protein-DNA interactions in this superfamily.</p>
},
	keywords = {Amino Acid Sequence, Bacterial Proteins, Dimerization, DNA-Binding Proteins, Helix-Turn-Helix Motifs, Models, Molecular, Protein Binding, Sequence Homology, Amino Acid, Structure-Activity Relationship, Transcription Factors},
	issn = {1740-1534},
	doi = {10.1038/nrmicro1717},
	author = {Schreiter, Eric R and Drennan, Catherine L}
}
