9C68
The CRISPR associated CARF-adenosine deaminase Cad1-CARF in the cA6 bound form
9C68 の概要
エントリーDOI | 10.2210/pdb9c68/pdb |
分子名称 | Adenosine deaminase domain-containing protein, RNA (5'-R(P*AP*AP*AP*AP*AP*A)-3') (3 entities in total) |
機能のキーワード | type-iii crispr defense system, carf-effector protein, adaptive immunity, deamination defense strategy, cyclic hexa-adenylate, antiviral protein-rna complex, antiviral protein/rna |
由来する生物種 | Bacteroidales bacterium 詳細 |
タンパク質・核酸の鎖数 | 3 |
化学式量合計 | 44068.53 |
構造登録者 | |
主引用文献 | Baca, C.F.,Majumder, P.,Hickling, J.H.,Ye, L.,Teplova, M.,Brady, S.F.,Patel, D.J.,Marraffini, L.A. The CRISPR-associated adenosine deaminase Cad1 converts ATP to ITP to provide antiviral immunity. Cell, 2024 Cited by PubMed Abstract: Type III CRISPR systems provide immunity against genetic invaders through the production of cyclic oligo-adenylate (cA) molecules that activate effector proteins that contain CRISPR-associated Rossman fold (CARF) domains. Here, we characterized the function and structure of an effector in which the CARF domain is fused to an adenosine deaminase domain, CRISPR-associated adenosine deaminase 1 (Cad1). We show that upon binding of cA or cA to its CARF domain, Cad1 converts ATP to ITP, both in vivo and in vitro. Cryoelectron microscopy (cryo-EM) structural studies on full-length Cad1 reveal an hexameric assembly composed of a trimer of dimers, with bound ATP at inter-domain sites required for activity and ATP/ITP within deaminase active sites. Upon synthesis of cA during phage infection, Cad1 activation leads to a growth arrest of the host that prevents viral propagation. Our findings reveal that CRISPR-Cas systems employ a wide range of molecular mechanisms beyond nucleic acid degradation to provide adaptive immunity in prokaryotes. PubMed: 39471810DOI: 10.1016/j.cell.2024.10.002 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.82 Å) |
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