9yix

Cryo-EM structure of SeAvs7 MCP EFTu1 tetrameric complex

spinqualitylabelsall models 9yix, resolution 3.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9yix is a 12 chain structure with sequence from Escherichia coli, Escherichia phage ZL19 and Salmonella enterica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.43Å Ligands: ATP, GTP, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A5H7DAD8_SALET Publication Abstract from PubMed Recognition of foreign molecules inside cells is critical for immunity across all domains of life. Proteins of the STAND NTPase superfamily(1,2), including eukaryotic NOD-like receptors, play a central role in this process(3,4). In bacteria and archaea, although several STAND families sense phage proteins(5-9), their functional diversity remains largely unexplored. Here we conduct a systematic phylogenetic analysis of prokaryotic STAND NTPases and identify at least 90 structurally distinct families associated with antiviral defence. We first show that the uncharacterized Avs7 family recognizes the major capsid protein (MCP) of tailed phages. Three cryogenic electron microscopy structures of Salmonella enterica Avs7 reveal an asymmetric, butterfly-shaped tetramer that assembles stepwise through large, MCP-induced conformational changes, incorporating bacterial elongation factor Tu (EF-Tu) as a structural component that enhances defence. Using genetic screens with a library of 687 phage genes, we further show that 13 additional STAND families sense 13 conserved phage proteins, encompassing most of the core structural and replicative components of tailed phages. These include 2 distinct MCP-sensing families (Avs8 and Avs10) and 11 others (Avs11-21), which recognize the portal, portal adaptor, tail nozzle, head-tail connector, tail terminator, tail tube protein, tail assembly chaperone, tape measure protein, DNA polymerase, helicase/RecA-type ATPase and single-stranded DNA annealing protein, respectively. Together, our findings reveal a mechanism of host-factor repurposing and establish structure-based pattern recognition as a fundamental strategy of bacterial immunity. Diverse bacterial pattern recognition receptors sense the core phage proteome.,Lee H, Luengo-Woods S, Zhang J, Makarova KS, Wolf YI, Chiu C, Evans SA, Chen J, Xiao H, Feng L, Koonin EV, Gao A Nature. 2026 Sep;657(8132):735-743. doi: 10.1038/s41586-026-10852-6. Epub 2026 , Jul 29. PMID:42527607 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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