6N7O

Crystal structure of GIL01 gp7

6N7O の概要

• エントリーDOI: 10.2210/pdb6n7o/pdb
• 分子名称: GIL01 gp7, IODIDE ION (3 entities in total)
• 機能のキーワード: viral protein
• 由来する生物種: Bacillus phage pGIL01
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 12530.57

構造登録者

Caveney, N.A.,Strynadka, N.C.J. (登録日: 2018-11-27, 公開日: 2019-05-15, 最終更新日: 2024-03-13)

主引用文献

Caveney, N.A.,Pavlin, A.,Caballero, G.,Bahun, M.,Hodnik, V.,de Castro, L.,Fornelos, N.,Butala, M.,Strynadka, N.C.J.
Structural Insights into Bacteriophage GIL01 gp7 Inhibition of Host LexA Repressor.
Structure, 27:1094-, 2019

PubMed Abstract: Bacteria identify and respond to DNA damage using the SOS response. LexA, a central repressor in the response, has been implicated in the regulation of lysogeny in various temperate bacteriophages. During infection of Bacillus thuringiensis with GIL01 bacteriophage, LexA represses the SOS response and the phage lytic cycle by binding DNA, an interaction further stabilized upon binding of a viral protein, gp7. Here we report the crystallographic structure of phage-borne gp7 at 1.7-Å resolution, and characterize the 4:2 stoichiometry and potential interaction with LexA using surface plasmon resonance, static light scattering, and small-angle X-ray scattering. These data suggest that gp7 stabilizes LexA binding to operator DNA via coordination of the N- and C-terminal domains of LexA. Furthermore, we have found that gp7 can interact with LexA from Staphylococcus aureus, a significant human pathogen. Our results provide structural evidence as to how phage factors can directly associate with LexA to modulate the SOS response.

PubMed: 31056420
DOI: 10.1016/j.str.2019.03.019

実験手法

X-RAY DIFFRACTION (1.7 Å)