+Search query
-Structure paper
Title | Structural basis for broad anti-phage immunity by DISARM. |
---|---|
Journal, issue, pages | Nat Commun, Vol. 13, Issue 1, Page 2987, Year 2022 |
Publish date | May 27, 2022 |
Authors | Jack P K Bravo / Cristian Aparicio-Maldonado / Franklin L Nobrega / Stan J J Brouns / David W Taylor / |
PubMed Abstract | In the evolutionary arms race against phage, bacteria have assembled a diverse arsenal of antiviral immune strategies. While the recently discovered DISARM (Defense Island System Associated with ...In the evolutionary arms race against phage, bacteria have assembled a diverse arsenal of antiviral immune strategies. While the recently discovered DISARM (Defense Island System Associated with Restriction-Modification) systems can provide protection against a wide range of phage, the molecular mechanisms that underpin broad antiviral targeting but avoiding autoimmunity remain enigmatic. Here, we report cryo-EM structures of the core DISARM complex, DrmAB, both alone and in complex with an unmethylated phage DNA mimetic. These structures reveal that DrmAB core complex is autoinhibited by a trigger loop (TL) within DrmA and binding to DNA substrates containing a 5' overhang dislodges the TL, initiating a long-range structural rearrangement for DrmAB activation. Together with structure-guided in vivo studies, our work provides insights into the mechanism of phage DNA recognition and specific activation of this widespread antiviral defense system. |
External links | Nat Commun / PubMed:35624106 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.3 - 3.4 Å |
Structure data | EMDB-24938, PDB-7s9v: EMDB-24939, PDB-7s9w: |
Chemicals | ChemComp-ADP: |
Source |
|
Keywords | IMMUNE SYSTEM / DISARM / Helicase |