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

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F14%3A43887443" target="_blank" >RIV/60076658:12310/14:43887443 - isvavai.cz</a>

Alternative codes found

RIV/67179843:_____/14:00437252 RIV/61388971:_____/14:00437252

Result on the web

<a href="http://link.springer.com/article/10.1007%2Fs00894-014-2334-1" target="_blank" >http://link.springer.com/article/10.1007%2Fs00894-014-2334-1</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1007/s00894-014-2334-1" target="_blank" >10.1007/s00894-014-2334-1</a>

Result language

angličtina

Original language name

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

Original language 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 subun

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

<a href="/en/project/GAP207%2F12%2F2323" target="_blank" >GAP207/12/2323: Endonuclease and translocase activity in type I restriction-modification complexes</a><br>

Continuities

S - Specificky vyzkum na vysokych skolach

Publication year

2014

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Journal of Molecular Modeling

ISSN

1610-2940

e-ISSN

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Volume of the periodical

20

Issue of the periodical within the volume

7

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

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UT code for WoS article

000339884800015

EID of the result in the Scopus database

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