Contributions of distinct quaternary contacts to cooperative operator binding by Mnt repressor.

Abstract excerpt

Mnt, a tetrameric repressor encoded by bacteriophage P22, uses N-domain dimers to contact each half of its operator site. Experiments with a double mutant and structural homology with the P22 Arc repressor suggest that contacts made by Arg-28 and stabilized by Glu-33 are largely responsible for dimer-dimer cooperativity in Mnt. These dimer-dimer contacts are energetically more important for operator binding than...

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