ArticleJournal of molecular modeling2014
Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I.
Article in Journal of molecular modeling, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- A residue of motif III positions the helicase domains of motor subunit HsdR in restriction-modification enzyme EcoR124I.Journal of molecular modeling · 2018Article
- The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation.PeerJ · 2017Article
- Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzyme.PloS one · 2015Article
- Molecular dynamics comparison of E. coli WrbA apoprotein and holoprotein.Journal of molecular modeling · 2014Article
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Authors and funding
12 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Restriction-modification systems protect bacteria from foreign DNA. Type I restriction-modification enzymes are multifunctional heteromeric complexes with DNA-cleavage and ATP-dependent DNA translocation activities located on endonuclease/motor subunit HsdR. The recent structure of the first intact motor subunit of the type I restriction enzyme from plasmid EcoR124I suggested a mechanism by which stalled translocation triggers DNA cleavage via a lysine residue on the endonuclease domain that contacts ATP bound between the two helicase domains. In the present work, molecular dynamics simulations are used to explore this proposal. Molecular dynamics simulations suggest that the Lys-ATP contact alternates with a contact with a nearby loop housing the conserved QxxxY motif that had been implicated in DNA cleavage. This model is tested here using in vivo and in vitro experiments. The results indicate how local interactions are transduced to domain motions within the endonuclease/motor subunit.
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