2FKD

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

2FKD の概要

• エントリーDOI: 10.2210/pdb2fkd/pdb
• 分子名称: Repressor protein CI (1 entity in total)
• 機能のキーワード: genetic switch, regulation, cooperativity, repressor, transcription regulator
• 由来する生物種: Enterobacteria phage 186
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 169033.47

構造登録者

Lewis, M. (登録日: 2006-01-04, 公開日: 2006-06-13, 最終更新日: 2024-02-14)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.7 Å)