Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	The CRISPR-associated adenosine deaminase Cad1 converts ATP to ITP to provide antiviral immunity.
Journal, issue, pages	Cell, Year 2024
Publish date	Oct 24, 2024
Authors	Christian F Baca / Puja Majumder / James H Hickling / Linzhi Ye / Marianna Teplova / Sean F Brady / Dinshaw J Patel / Luciano A Marraffini /
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 ...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.
External links	Cell / PubMed:39471810
Methods	EM (single particle) / X-ray diffraction
Resolution	1.82 - 3.6 Å
Structure data	45241 9c67 EMDB-45241, PDB-9c67: cryoEM structure of CRISPR associated effector, CARF-Adenosine deaminase 1, Cad1, in apo form Method: EM (single particle) / Resolution: 3.6 Å 45244 9c6c EMDB-45244, PDB-9c6c: cryoEM structure of CRISPR associated effector, CARF-Adenosine deaminase 1, Cad1, in apo form with ATP (symmetric sites). Method: EM (single particle) / Resolution: 3.4 Å 45245 9c6f EMDB-45245, PDB-9c6f: cryoEM structure of CRISPR associated effector, CARF-Adenosine deaminase 1, Cad1, in apo form with ATP (Asymmetric sites). Method: EM (single particle) / Resolution: 3.6 Å 45277 9c77 EMDB-45277, PDB-9c77: cryoEM structure of CRISPR associated effector, CARF-Adenosine deaminase 1, Cad1, in cA4 bound form with ATP. Method: EM (single particle) / Resolution: 3.2 Å 45466 9cdb EMDB-45466, PDB-9cdb: CryoEM structure of CRISPR associated effector, CARF-Adenosine deaminase 1, Cad1, in cA6 (partial density) bound form with ATP (partial density). Method: EM (single particle) / Resolution: 3.6 Å PDB-9c68: The CRISPR associated CARF-adenosine deaminase Cad1-CARF in the cA6 bound form Method: X-RAY DIFFRACTION / Resolution: 1.82 Å PDB-9c69: The CRISPR associated CARF-adenosine deaminase, Cad1-CARF in the cA4 bound form Method: X-RAY DIFFRACTION / Resolution: 2.4 Å PDB-9c6a: The CRISPR associated adenosine deaminase Cad1-CARF in the apo form Method: X-RAY DIFFRACTION / Resolution: 3.6 Å
Chemicals	ChemComp-MG: Unknown entry ChemComp-HOH: WATER ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM
Source	Bacteriodale bacterium (bacteria) bacteroidales bacterium (bacteria) bacteroidale bacteria (bacteria)
Keywords	ANTIVIRAL PROTEIN / Antiphage defense / CRISPR / Deamination / CARF-Adenosine deaminase / Antiviral Protein/RNA / Type-III CRISPR defense system / CARF-effector protein / adaptive immunity / deamination defense strategy / cyclic Hexa-adenylate / Antiviral Protein-RNA complex / CYTOSOLIC PROTEIN / cyclic Tetra-adenylate / ATP / cA4