Structural basis for translocation by AddAB helicase–nuclease and its arrest at χ sites
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Title
Structural basis for translocation by AddAB helicase–nuclease and its arrest at χ sites
Authors
Keywords
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Journal
NATURE
Volume 508, Issue 7496, Pages 416-419
Publisher
Springer Nature
Online
2014-03-17
DOI
10.1038/nature13037
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- Crystal structures of exonuclease in complex with DNA suggest an electrostatic ratchet mechanism for processivity
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- Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor
- (2010) Colin G Wu et al. NATURE STRUCTURAL & MOLECULAR BIOLOGY
- The AddAB helicase–nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain
- (2010) Joseph T.P. Yeeles et al. NUCLEIC ACIDS RESEARCH
- An Iron-Sulfur Cluster Is Essential for the Binding of Broken DNA by AddAB-type Helicase-Nucleases
- (2009) Joseph T. P. Yeeles et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Characterization of the Mycobacterial AdnAB DNA Motor Provides Insights into the Evolution of Bacterial Motor-Nuclease Machines
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- RecBCD Enzyme and the Repair of Double-Stranded DNA Breaks
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