Chapter 1: Variation in form and function the helix-turn-helix regulators of the GntR superfamily.

  title={Chapter 1: Variation in form and function the helix-turn-helix regulators of the GntR superfamily.},
  author={Paul A Hoskisson and S{\'e}bastien Rigali},
  journal={Advances in applied microbiology},
One of the most abundant and widely distributed groups of Helix-turn-helix (HTH) transcription factors is the metabolite-responsive GntR family of regulators (>8500 members in the Pfam database; Jan 2009). These proteins contain a DNA-binding HTH domain at the N terminus of the protein and an effector-binding and/or oligomerisation domain at the C terminus, where upon on binding an effector molecule, a conformational change occurs in the protein which influences the DNA-binding properties of… CONTINUE READING
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The Pfam protein families database

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View 10 Excerpts
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A new family of bacterial regulatory proteins.

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