9ntn

Structure of Cap10-CdnD complex containing NDG modification

spinqualitylabelsall models 9ntn, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9ntn is a 4 chain structure with sequence from Hyphomicrobiales. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.43Å Ligands: 2KA, COA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 7-deazapurines are nucleobase analogs essential for nucleic acid modifications in nearly all cellular life. Here, we discover a role for 7-deazapurines in protein modification within type IV CBASS anti-phage defense and define functions for CBASS ancillary proteins Cap9 and Cap10 in nucleobase-protein conjugation. A structure of Cap10 reveals a tRNA transglycosylase-family enzyme remodeled to bind the modified N-terminus of a partner cGAS/DncV-like nucleotidyltransferase linked to a 7-amido-7-deazaguanine (NDG) nucleobase. The structure of Cap9 explains how this QueC-like enzyme co-opts a 7-deazapurine biosynthetic reaction mechanism for NDG conjugation. We demonstrate that Cap9, Cap10, and NDG conjugation are essential for host defense against phage infection. Our results define a previously unknown 7-deazapurine protein modification and explain how nucleobase biosynthetic machinery has been repurposed for antiviral immunity. Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity.,Wassarman DR, Pfaff P, Paulo JA, Gygi SP, Shokat KM, Kranzusch PJ bioRxiv [Preprint]. 2025 Apr 6:2025.04.06.647259. doi: 10.1101/2025.04.06.647259. PMID:40236162 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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