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9NTN

Structure of Cap10-CdnD complex containing NDG modification

Summary for 9NTN
Entry DOI10.2210/pdb9ntn/pdb
DescriptorCap10, CdnD, COENZYME A, ... (5 entities in total)
Functional Keywordscd-ntase, quec, cbass, antiviral protein
Biological sourceHyphomicrobiales
More
Total number of polymer chains4
Total formula weight145724.73
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 citationWassarman, 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: 40236162
DOI: 10.1101/2025.04.06.647259
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.43 Å)
Structure validation

239149

数据于2025-07-23公开中

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