8u0u | pdb_00008u0u

DdmD dimer in complex with ssDNA

spinqualitylabelsall models 8u0u, resolution 3.04Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8u0u is a 4 chain structure with sequence from Vibrio cholerae and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.04Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B9TSM3_VIBCL Publication Abstract from PubMed Although eukaryotic Argonautes have a pivotal role in post-transcriptional gene regulation through nucleic acid cleavage, some short prokaryotic Argonaute variants (pAgos) rely on auxiliary nuclease factors for efficient foreign DNA degradation(1). Here we reveal the activation pathway of the DNA defence module DdmDE system, which rapidly eliminates small, multicopy plasmids from the Vibrio cholerae seventh pandemic strain (7PET)(2). Through a combination of cryo-electron microscopy, biochemistry and in vivo plasmid clearance assays, we demonstrate that DdmE is a catalytically inactive, DNA-guided, DNA-targeting pAgo with a distinctive insertion domain. We observe that the helicase-nuclease DdmD transitions from an autoinhibited, dimeric complex to a monomeric state upon loading of single-stranded DNA targets. Furthermore, the complete structure of the DdmDE-guide-target handover complex provides a comprehensive view into how DNA recognition triggers processive plasmid destruction. Our work establishes a mechanistic foundation for how pAgos utilize ancillary factors to achieve plasmid clearance, and provides insights into anti-plasmid immunity in bacteria. Plasmid targeting and destruction by the DdmDE bacterial defence system.,Bravo JPK, Ramos DA, Fregoso Ocampo R, Ingram C, Taylor DW Nature. 2024 Jun;630(8018):961-967. doi: 10.1038/s41586-024-07515-9. Epub 2024 , May 13. PMID:38740055 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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