1f39
From Proteopedia
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CRYSTAL STRUCTURE OF THE LAMBDA REPRESSOR C-TERMINAL DOMAIN
Overview
Interactions between transcription factors bound to separate operator, sites commonly play an important role in gene regulation by mediating, cooperative binding to the DNA. However, few detailed structural models, for understanding the molecular basis of such cooperativity are available., The c1 repressor of bacteriophage lambda is a classic example of a protein, that binds to its operator sites cooperatively. The C-terminal domain of, the repressor mediates dimerization as well as a dimer-dimer interaction, that results in the cooperative binding of two repressor dimers to, adjacent operator sites. Here, we present the x-ray crystal structure of, the lambda repressor C-terminal domain determined by multiwavelength, anomalous diffraction. Remarkably, the interactions that mediate, cooperativity are captured in the crystal, where two dimers associate, about a 2-fold axis of symmetry. Based on the structure and previous, genetic and biochemical data, we present a model for the cooperative, binding of two lambda repressor dimers at adjacent operator sites.
About this Structure
1F39 is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.
Reference
Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding., Bell CE, Frescura P, Hochschild A, Lewis M, Cell. 2000 Jun 23;101(7):801-11. PMID:10892750
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