9GCU

Rho-P167L-ATP gamma S

Summary for 9GCU

• Entry DOI: 10.2210/pdb9gcu/pdb
• Related: 8PEU 8PEW 8PEX 8PEY 9GCS 9GCT
• EMDB information: 17637 17639 17640 17641 51235 51236 51237
• Descriptor: Transcription termination factor Rho, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: transcription termination, transcription
• Biological source: Escherichia coli
• Total number of polymer chains: 6
• Total formula weight: 284774.80

Authors

Gjorgjevikj, D.,Wahl, M.C.,Hilal, T.,Loll, B. (deposition date: 2024-08-02, release date: 2024-10-09, Last modification date: 2025-01-22)

Primary citation

Gjorgjevikj, D.,Kumar, N.,Wang, B.,Hilal, T.,Said, N.,Loll, B.,Artsimovitch, I.,Sen, R.,Wahl, M.C.
The Psu protein of phage satellite P4 inhibits transcription termination factor rho by forced hyper-oligomerization.
Nat Commun, 16:550-550, 2025

PubMed Abstract: Many bacteriophages modulate host transcription to favor expression of their own genomes. Phage satellite P4 polarity suppression protein, Psu, a building block of the viral capsid, inhibits hexameric transcription termination factor, ρ, by presently unknown mechanisms. Our cryogenic electron microscopy structures of ρ-Psu complexes show that Psu dimers clamp two inactive, open ρ rings and promote their expansion to higher-oligomeric states. ATPase, nucleotide binding and nucleic acid binding studies revealed that Psu hinders ρ ring closure and traps nucleotides in their binding pockets on ρ. Structure-guided mutagenesis in combination with growth, pull-down, and termination assays further delineated the functional ρ-Psu interfaces in vivo. Bioinformatic analyses revealed that Psu is associated with a wide variety of phage defense systems across Enterobacteriaceae, suggesting that Psu may regulate expression of anti-phage genes. Our findings show that modulation of the ρ oligomeric state via diverse strategies is a pervasive gene regulatory principle in bacteria.

PubMed: 39788982
DOI: 10.1038/s41467-025-55897-9

Experimental method

ELECTRON MICROSCOPY (2.8 Å)