1F39

CRYSTAL STRUCTURE OF THE LAMBDA REPRESSOR C-TERMINAL DOMAIN

Summary for 1F39

• Entry DOI: 10.2210/pdb1f39/pdb
• Descriptor: REPRESSOR PROTEIN CI (2 entities in total)
• Functional Keywords: cooperative operator binding, reca-mediated self-cleavage, gene regulation, viral protein
• Biological source: Enterobacteria phage lambda
• Total number of polymer chains: 2
• Total formula weight: 21862.66

Authors

Bell, C.E.,Frescura, P.,Hochschild, A.,Lewis, M. (deposition date: 2000-06-01, release date: 2000-07-26, Last modification date: 2024-10-30)

Primary citation

Bell, C.E.,Frescura, P.,Hochschild, A.,Lewis, M.
Crystal structure of the lambda repressor C-terminal domain provides a model for cooperative operator binding.
Cell(Cambridge,Mass.), 101:801-811, 2000

PubMed Abstract: 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.

PubMed: 10892750
DOI: 10.1016/S0092-8674(00)80891-0

Experimental method

X-RAY DIFFRACTION (1.9 Å)