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9EZX

Vibrio cholerae DdmD apo complex

Summary for 9EZX
Entry DOI10.2210/pdb9ezx/pdb
EMDB information50090
DescriptorHelicase/UvrB N-terminal domain-containing protein (1 entity in total)
Functional Keywordshelicase, nuclease, complex, effector, immune system
Biological sourceVibrio cholerae
Total number of polymer chains2
Total formula weight272855.19
Authors
Loeff, L.,Jinek, M. (deposition date: 2024-04-14, release date: 2024-06-19, Last modification date: 2024-07-24)
Primary citationLoeff, 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. In this study, we used cryogenic electron microscopy to determine the mechanistic basis for plasmid defense by DdmDE. The helicase-nuclease DdmD adopts an autoinhibited dimeric architecture. The prokaryotic Argonaute protein DdmE uses a DNA guide to target plasmid DNA. The 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 nontarget DNA strand. In vitro studies indicate 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: 38870273
DOI: 10.1126/science.adq0534
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.55 Å)
Structure validation

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PDB entries from 2024-11-20

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