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	A DNA-gated molecular guard controls bacterial Hailong anti-phage defence.
Journal, issue, pages	Nature, Vol. 643, Issue 8072, Page 794-800, Year 2025
Publish date	Apr 30, 2025
Authors	Joel M J Tan / Sarah Melamed / Joshua C Cofsky / Deepsing Syangtan / Samuel J Hobbs / Josefina Del Mármol / Marco Jost / Andrew C Kruse / Rotem Sorek / Philip J Kranzusch /
PubMed Abstract	Animal and bacterial cells use nucleotidyltransferase (NTase) enzymes to respond to viral infection and control major forms of immune signalling including cGAS-STING innate immunity and CBASS anti- ...Animal and bacterial cells use nucleotidyltransferase (NTase) enzymes to respond to viral infection and control major forms of immune signalling including cGAS-STING innate immunity and CBASS anti-phage defence. Here we discover a family of bacterial defence systems, which we name Hailong, that use NTase enzymes to constitutively synthesize DNA signals and guard against phage infection. Hailong protein B (HalB) is an NTase that converts deoxy-ATP into single-stranded DNA oligomers. A series of X-ray crystal structures define a stepwise mechanism of HalB DNA synthesis initiated by a C-terminal tyrosine residue that enables de novo enzymatic priming. We show that HalB DNA signals bind to and repress activation of a partnering Hailong protein A (HalA) effector complex. A 2.0-Å cryo-electron microscopy structure of the HalA-DNA complex reveals a membrane protein with a conserved ion channel domain and a unique crown domain that binds the DNA signal and gates activation. Analysing Hailong defence in vivo, we demonstrate that viral DNA exonucleases required for phage replication trigger release of the primed HalA complex and induce protective host cell growth arrest. Our results explain how inhibitory nucleotide immune signals can serve as molecular guards against phage infection and expand the mechanisms NTase enzymes use to control antiviral immunity.
External links	Nature / PubMed:40306316 / PubMed Central
Methods	EM (single particle) / X-ray diffraction
Resolution	1.88 - 2.41 Å
Structure data	49920 9nyi EMDB-49920: Structure of Hailong HalA in complex with oligodeoxyadenylate PDB-9nyi: Structure of HalA in complex with oligodeoxyadenylate Method: EM (single particle) / Resolution: 1.98 Å PDB-9dbh: Structure of Hailong HalB in complex with oligodeoxyadenylate Method: X-RAY DIFFRACTION / Resolution: 1.88 Å PDB-9dbi: Structure of Hailong HalB D21A/D23A mutant Method: X-RAY DIFFRACTION / Resolution: 1.99 Å PDB-9dbj: Structure of Hailong HalB R164A mutant with non-hydrolyzable dATP Method: X-RAY DIFFRACTION / Resolution: 2.41 Å
Chemicals	ChemComp-MN: Unknown entry ChemComp-HOH: WATER ChemComp-PO4: PHOSPHATE ION PDB-1a3g: BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI ChemComp-F2A: 2'-deoxy-5'-O-[(S)-hydroxy{[(S)-hydroxy(phosphonooxy)phosphoryl]methyl}phosphoryl]adenosine PDB-1a3h: ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHERANS AT 1.6A RESOLUTION ChemComp-D5M: 2'-DEOXYADENOSINE-5'-MONOPHOSPHATE
Source	rhodobacteraceae bacterium qy30 (bacteria) dna molecule (others)
Keywords	ANTIVIRAL PROTEIN/DNA / Hailong / nucleotidyltransferase / oligodeoxyadenylate / anti-phage defense / ANTIVIRAL PROTEIN / ANTIVIRAL PROTEIN-DNA complex / ion channel