9EZY
Vibrio cholerae DdmD-DdmE holo complex
Summary for 9EZY
| Entry DOI | 10.2210/pdb9ezy/pdb |
| EMDB information | 50091 |
| Descriptor | Helicase/UvrB N-terminal domain-containing protein, Vibrio cholerae DdmE, 14 nucleotide DNA guide with terminal 5' phosphate, ... (6 entities in total) |
| Functional Keywords | helicase, nuclease, complex, effector, argonaute, immune system |
| Biological source | Vibrio cholerae More |
| Total number of polymer chains | 5 |
| Total formula weight | 261134.11 |
| Authors | |
| Primary citation | Loeff, L.,Adams, D.W.,Chanez, C.,Stutzmann, S.,Righi, L.,Blokesch, M.,Jinek, M. Molecular mechanism of plasmid elimination by the DdmDE defense system. Science, 385:188-194, 2024 Cited by PubMed Abstract: Seventh pandemic strains contain two pathogenicity islands that encode the DNA defense modules DdmABC and DdmDE. Here we use cryogenic electron microscopy to reveal the mechanistic basis for plasmid defense by DdmDE. A structure of the DdmD helicase-nuclease reveals it adopts an auto-inhibited dimeric architecture. The prokaryotic Argonaute protein DdmE uses a DNA guide to target plasmid DNA. A structure of the DdmDE complex, validated by in vivo mutational studies, shows that DNA binding by DdmE triggers disassembly of the DdmD dimer and loading of monomeric DdmD onto the non-target DNA strand. In vitro studies reveal that DdmD translocates in the 5'-to-3' direction, while partially degrading the plasmid DNA. These findings provide critical insights into the mechanism of DdmDE systems in plasmid elimination. PubMed: 38870273DOI: 10.1126/science.adq0534 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.56 Å) |
Structure validation
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