About: Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I Goto Sponge Distinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
Description	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. 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. (en)
Title	Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I (en)
skos:prefLabel	Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124I (en)
skos:notation	RIV/67179843:_____/14:00437252!RIV15-GA0-67179843
http://linked.open...avai/riv/aktivita	I P S
http://linked.open...avai/riv/aktivity	I, P(GAP207/12/2323), S
http://linked.open...iv/cisloPeriodika	7
http://linked.open...vai/riv/dodaniDat	2015
http://linked.open...aciTvurceVysledku	Shamayeva, Katerina Cséfalvay, Eva Řeha, David Khabiri, Morteza Ettrich, Rüdiger Sinha, Dhiraj
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Centrum výzkumu globální změny AV ČR, v. v. i.
http://linked.open...dnocenehoVysledku	22373
http://linked.open...ai/riv/idVysledku	RIV/67179843:_____/14:00437252
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	DNA restriction enzymes; Molecular modeling; QM/MM calculations; principal components analysis; E. coli; Multisubunit enzyme complex; Correlated loop motions (en)
http://linked.open.../riv/klicoveSlovo	Molecular modeling Correlated loop motions DNA restriction enzymes Multisubunit enzyme complex E. coli principal components analysis QM/MM calculations
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[87C10D1467EF]
http://linked.open...i/riv/nazevZdroje	Journal of Molecular Modeling
http://linked.open...in/vavai/riv/obor	EH
http://linked.open...ichTvurcuVysledku	6 (xsd:int)
http://linked.open...cetTvurcuVysledku	12 (xsd:int)
http://linked.open...vavai/riv/projekt	Endonuclease and translocase activity in type I restriction-modification complexes
http://linked.open...UplatneniVysledku	2014
http://linked.open...v/svazekPeriodika	20
http://linked.open...iv/tvurceVysledku	Ettrich, Rüdiger Khabiri, Morteza Weiserová, Marie Carey, J. Řeha, David Cséfalvay, Eva Bialevich, V. Guzanová, Alena Milbar, N. Ramasubramani, V. Shamayeva, Katerina Sinha, Dhiraj
http://linked.open...ain/vavai/riv/wos	000339884800015
issn	1610-2940
number of pages	13 (xsd:int)
http://bibframe.org/vocab/doi	10.1007/s00894-014-2334-1

Faceted Search & Find service v1.16.118 as of Jun 21 2024

Alternative Linked Data Documents: ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 112 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software