7TB5

Structure of P. aeruginosa PA17 CapW

Summary for 7TB5

• Entry DOI: 10.2210/pdb7tb5/pdb
• Descriptor: WYL domain-containing protein, SULFATE ION (3 entities in total)
• Functional Keywords: helix-turn-helix, winged helix, wyl, transcription factor, dna binding protein
• Biological source: Pseudomonas aeruginosa
• Total number of polymer chains: 1
• Total formula weight: 35016.72

Authors

Blankenchip, C.L.,Nguyen, J.V.,Lau, R.K.,Ye, Q.,Corbett, K.D. (deposition date: 2021-12-21, release date: 2022-01-19, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.3 Å)