9Y9C

Cryo-EM map of the in vitro reconstituted RAZR:GP77 complex with AlphaFold-predicted models fitted into the density.

This is a non-PDB format compatible entry.

Summary for 9Y9C

• Entry DOI: 10.2210/pdb9y9c/pdb
• EMDB information: 72693
• Descriptor: Gp77, DUF4145 domain-containing protein, ZINC ION (3 entities in total)
• Functional Keywords: phage-bacterial defense complex, abortive infection ring-activated zinc-finger rnase (razr), rna binding protein
• Biological source: Escherichia phage SECphi27; More
• Total number of polymer chains: 48
• Total formula weight: 1205953.97

Authors

Lyu, Y.,Zhang, T.,Laub, M.,Ghanbarpour, A. (deposition date: 2025-09-14, release date: 2025-12-24, Last modification date: 2026-07-22)

Primary citation

Zhang, T.,Lyu, Y.,Beck, C.R.,Iqbal, N.,Barbosa, R.,Ghanbarpour, A.,Laub, M.T.
Bacterial immune activation via supramolecular assembly with phage triggers.
Nature, 651:1051-1059, 2026

PubMed Abstract: Bacteria use diverse mechanisms to protect themselves against phages. Many antiphage systems form large oligomeric complexes, but how oligomerization is regulated during phage infection remains mostly unknown. Here we demonstrate that the bacterial immunity protein ring-activated zinc-finger RNase (RAZR) assembles into an active, 24-meric ring around the circumference of large ring structures formed by two unrelated phage proteins: a putative recombinase and a portal protein. Each multi-layered, megadalton-scale complex enables RAZR to cleave RNA nonspecifically to inhibit translation and restrict phage propagation. The recognition of unrelated phage proteins that form rings with similar diameters indicates that these proteins not only bind to RAZR but also enforce a geometry crucial to activation. The lack of large ring structures in the host probably prevents auto-immunity and RAZR activation before infection. The infection-triggered oligomerization of RAZR mirrors pathogen-induced oligomerization in eukaryotic innate immune complexes, underscoring a common principle of immunity across biology.

PubMed: 41639456
DOI: 10.1038/s41586-025-10060-8

Experimental method

ELECTRON MICROSCOPY (3.5 Å)