9NTN

Structure of Cap10-CdnD complex containing NDG modification

9NTN の概要

• エントリーDOI: 10.2210/pdb9ntn/pdb
• 分子名称: Cap10, CdnD, COENZYME A, ... (5 entities in total)
• 機能のキーワード: cd-ntase, quec, cbass, antiviral protein
• 由来する生物種: Hyphomicrobiales; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 145724.73

構造登録者

Wassarman, D.R.,Pfaff, P.,Paulo, J.A.,Gygi, S.P.,Shokat, K.M.,Kranzusch, P.J. (登録日: 2025-03-18, 公開日: 2025-05-07, 最終更新日: 2025-10-08)

主引用文献

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.
Science, 389:1347-1352, 2025

PubMed Abstract: 7-Deazapurines are nucleobase analogs essential for nucleic acid modifications in nearly all cellular life. In this study, we discovered a role for 7-deazapurines in protein modification within type IV cyclic oligonucleotide-based antiviral signaling system (CBASS) antiphage defense and defined functions for CBASS ancillary proteins Cap9 and Cap10 in nucleobase-protein conjugation. A structure of Cap10 revealed a transfer RNA transglycosylase family enzyme remodeled to bind a partner cGAS/DncV-like nucleotidyltransferase that is modified with an N-terminal 7-amido-7-deazaguanine (NDG) nucleobase. A structure of Cap9 explained how this QueC-like enzyme co-opts a 7-deazapurine biosynthetic reaction to install NDG. We show that Cap9, Cap10, and protein deazaguanylation are essential for host defense against phage infection. Our results define a 7-deazapurine protein modification and explain how nucleobase biosynthetic machinery has been repurposed for antiviral immunity.

PubMed: 40997174
DOI: 10.1126/science.adx6053

実験手法

X-RAY DIFFRACTION (2.43 Å)