Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: Evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes

Journal of Molecular Biology

Volumn 277, Issue 2, 1998, Pages 257-271

  Hall, Mark C ^a   Özsoy, A Zeynep ^a   Matson, Steven W ^a  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

ATP hydrolysis; DNA binding; Helicase; Helicase motif; UvrD

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ARGININE; DNA BINDING PROTEIN; HELICASE; METHYL GROUP; SINGLE STRANDED DNA; THREONINE;

ALLELE; ARTICLE; BASE MISPAIRING; CONFORMATIONAL TRANSITION; DNA BINDING; ENZYME CONFORMATION; ESCHERICHIA COLI; EXCISION REPAIR; GENETIC CONSERVATION; HYDROLYSIS; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL; SITE DIRECTED MUTAGENESIS;

EID: 0032571396     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1614     Document Type: Article

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