Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I
Jazyk angličtina Země Německo Médium print-electronic
Typ dokumentu časopisecké články, práce podpořená grantem, Research Support, U.S. Gov't, Non-P.H.S.
- MeSH
- adenosintrifosfát chemie metabolismus MeSH
- aminokyselinové motivy MeSH
- DNA chemie metabolismus MeSH
- fenotyp MeSH
- genotyp MeSH
- hydrolýza MeSH
- katalýza MeSH
- kinetika MeSH
- konzervovaná sekvence MeSH
- kvantová teorie MeSH
- lysin MeSH
- mutace MeSH
- mutageneze cílená MeSH
- restrikční endonukleasy typu I chemie genetika metabolismus MeSH
- simulace molekulární dynamiky MeSH
- terciární struktura proteinů MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- vztahy mezi strukturou a aktivitou MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Research Support, U.S. Gov't, Non-P.H.S. MeSH
- Názvy látek
- adenosintrifosfát MeSH
- DNA MeSH
- endodeoxyribonuclease EcoR124I MeSH Prohlížeč
- lysin MeSH
- restrikční endonukleasy typu I MeSH
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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