2FKD

Crystal Structure of the C-terminal domain of Bacteriophage 186 repressor

Summary for 2FKD

• Entry DOI: 10.2210/pdb2fkd/pdb
• Descriptor: Repressor protein CI (1 entity in total)
• Functional Keywords: genetic switch, regulation, cooperativity, repressor, transcription regulator
• Biological source: Enterobacteria phage 186
• Total number of polymer chains: 14
• Total formula weight: 169033.47

Authors

Lewis, M. (deposition date: 2006-01-04, release date: 2006-06-13, Last modification date: 2024-02-14)

Primary citation

Pinkett, H.W.,Shearwin, K.E.,Stayrook, S.,Dodd, I.B.,Burr, T.,Hochschild, A.,Egan, J.B.,Lewis, M.
The structural basis of cooperative regulation at an alternate genetic switch.
Mol.Cell, 21:605-615, 2006

PubMed Abstract: Bacteriophage lambda is a paradigm for understanding the role of cooperativity in gene regulation. Comparison of the regulatory regions of lambda and the unrelated temperate bacteriophage 186 provides insight into alternate ways to assemble functional genetic switches. The structure of the C-terminal domain of the 186 repressor, determined at 2.7 A resolution, reveals an unusual heptamer of dimers, consistent with presented genetic studies. In addition, the structure of a cooperativity mutant of the full-length 186 repressor, identified by genetic screens, was solved to 1.95 A resolution. These structures provide a molecular basis for understanding lysogenic regulation in 186. Whereas the overall fold of the 186 and lambda repressor monomers is remarkably similar, the way the two repressors cooperatively assemble is quite different and explains in part the differences in their regulatory activity.

PubMed: 16507359
DOI: 10.1016/j.molcel.2006.01.019

Experimental method

X-RAY DIFFRACTION (2.7 Å)