1F39

CRYSTAL STRUCTURE OF THE LAMBDA REPRESSOR C-TERMINAL DOMAIN

1F39 の概要

• エントリーDOI: 10.2210/pdb1f39/pdb
• 分子名称: REPRESSOR PROTEIN CI (2 entities in total)
• 機能のキーワード: cooperative operator binding, reca-mediated self-cleavage, gene regulation, viral protein
• 由来する生物種: Enterobacteria phage lambda
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 21862.66

構造登録者

Bell, C.E.,Frescura, P.,Hochschild, A.,Lewis, M. (登録日: 2000-06-01, 公開日: 2000-07-26, 最終更新日: 2024-10-30)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.9 Å)