9NTN
Structure of Cap10-CdnD complex containing NDG modification
Summary for 9NTN
Entry DOI | 10.2210/pdb9ntn/pdb |
Descriptor | Cap10, CdnD, COENZYME A, ... (5 entities in total) |
Functional Keywords | cd-ntase, quec, cbass, antiviral protein |
Biological source | Hyphomicrobiales More |
Total number of polymer chains | 4 |
Total formula weight | 145724.73 |
Authors | Wassarman, D.R.,Pfaff, P.,Paulo, J.A.,Gygi, S.P.,Shokat, K.M.,Kranzusch, P.J. (deposition date: 2025-03-18, release date: 2025-05-07) |
Primary citation | Wassarman, D.R.,Pfaff, P.,Paulo, J.A.,Gygi, S.P.,Shokat, K.M.,Kranzusch, P.J. Deazaguanylation is a nucleobase-protein conjugation required for type IV CBASS immunity. Biorxiv, 2025 Cited by PubMed Abstract: 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. PubMed: 40236162DOI: 10.1101/2025.04.06.647259 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.43 Å) |
Structure validation
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