Structure of the motor subunit of type I restriction-modification complex EcoR124I
about
SF1 and SF2 helicases: family mattersExtensive DNA mimicry by the ArdA anti-restriction protein and its role in the spread of antibiotic resistanceThe fragment structure of a putative HsdR subunit of a type I restriction enzyme from Vibrio vulnificus YJ016: implications for DNA restriction and translocation activityCharacterization and crystal structure of the type IIG restriction endonuclease RM.BpuSIStructural characterization of a modification subunit of a putative type I restriction enzyme from Vibrio vulnificus YJ016pHluorin-assisted expression, purification, crystallization and X-ray diffraction data analysis of the C-terminal domain of the HsdR subunit of the Escherichia coli type I restriction-modification system EcoR124I.Structural and functional analysis of the symmetrical Type I restriction endonuclease R.EcoR124I(NT).Structure and operation of the DNA-translocating type I DNA restriction enzymes.Functional coupling of duplex translocation to DNA cleavage in a type I restriction enzymeSequence, structure and functional diversity of PD-(D/E)XK phosphodiesterase superfamilyGenome-wide survey of codons under diversifying selection in a highly recombining bacterial species, Helicobacter pyloriSuperfamily 2 helicasesCloning, crystallization and preliminary X-ray diffraction analysis of an intact DNA methyltransferase of a type I restriction-modification enzyme from Vibrio vulnificus.Maintaining a sense of direction during long-range communication on DNA.Nucleases: diversity of structure, function and mechanism.Duplex RNA activated ATPases (DRAs): platforms for RNA sensing, signaling and processing.Type I restriction enzymes and their relatives.The helical domain of the EcoR124I motor subunit participates in ATPase activity and dsDNA translocation.Crystal structure of the R-protein of the multisubunit ATP-dependent restriction endonuclease NgoAVII.Structural and functional analysis of the engineered type I DNA methyltransferase EcoR124I(NT)Type III restriction endonuclease EcoP15I is a heterotrimeric complex containing one Res subunit with several DNA-binding regions and ATPase activity.Structural basis underlying complex assembly and conformational transition of the type I R-M system.The H-subunit of the restriction endonuclease CglI contains a prototype DEAD-Z1 helicase-like motor.Interdomain communication in the endonuclease/motor subunit of type I restriction-modification enzyme EcoR124IA model for the evolution of prokaryotic DNA restriction-modification systems based upon the structural malleability of Type I restriction-modification enzymes
P2860
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P2860
Structure of the motor subunit of type I restriction-modification complex EcoR124I
description
2009 nî lūn-bûn
@nan
2009 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@ast
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@en
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@nl
type
label
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@ast
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@en
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@nl
prefLabel
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@ast
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@en
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@nl
P2093
P356
P1476
Structure of the motor subunit of type I restriction-modification complex EcoR124I
@en
P2093
Eva Csefalvay
Ivana Kuta Smatanova
Jannette Carey
Mikalai Lapkouski
Pavel Janscak
P2888
P356
10.1038/NSMB.1523
P577
2008-12-14T00:00:00Z
P5875
P6179
1052602488