7TB6

Structure of S. maltophilia CapW

7TB6 の概要

• エントリーDOI: 10.2210/pdb7tb6/pdb
• 分子名称: S. maltophilia CapW, SULFATE ION (3 entities in total)
• 機能のキーワード: helix-turn-helix, winged helix, wyl, transcription factor, dna binding protein
• 由来する生物種: Stenotrophomonas maltophilia
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34661.19

構造登録者

Blankenchip, C.L.,Nguyen, J.V.,Lau, R.K.,Ye, Q.,Corbett, K.D. (登録日: 2021-12-21, 公開日: 2022-01-19, 最終更新日: 2023-10-18)

主引用文献

Blankenchip, C.L.,Nguyen, J.V.,Lau, R.K.,Ye, Q.,Gu, Y.,Corbett, K.D.
Control of bacterial immune signaling by a WYL domain transcription factor.
Nucleic Acids Res., 50:5239-5250, 2022

PubMed Abstract: Bacteria use diverse immune systems to defend themselves from ubiquitous viruses termed bacteriophages (phages). Many anti-phage systems function by abortive infection to kill a phage-infected cell, raising the question of how they are regulated to avoid cell killing outside the context of infection. Here, we identify a transcription factor associated with the widespread CBASS bacterial immune system, that we term CapW. CapW forms a homodimer and binds a palindromic DNA sequence in the CBASS promoter region. Two crystal structures of CapW suggest that the protein switches from an unliganded, DNA binding-competent state to a ligand-bound state unable to bind DNA. We show that CapW strongly represses CBASS gene expression in uninfected cells, and that phage infection causes increased CBASS expression in a CapW-dependent manner. Unexpectedly, this CapW-dependent increase in CBASS expression is not required for robust anti-phage activity, suggesting that CapW may mediate CBASS activation and cell death in response to a signal other than phage infection. Our results parallel concurrent reports on the structure and activity of BrxR, a transcription factor associated with the BREX anti-phage system, suggesting that CapW and BrxR are members of a family of universal defense signaling proteins.

PubMed: 35536256
DOI: 10.1093/nar/gkac343

実験手法

X-RAY DIFFRACTION (1.89 Å)