Structural basis for translocation by AddAB helicase–nuclease and its arrest at χ sites

A dual-function helicase–nuclease, typified by RecBCD in Escherichia coli , acts on free DNA ends during bacterial double-stranded break repair until it reaches a χ sequence at which it pauses before continuing with modified enzymatic properties; here several crystal structures of the related AddAB...

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Bibliographic Details
Published in:	Nature (London) Vol. 508; no. 7496; pp. 416 - 419
Main Authors:	Krajewski, Wojciech W., Fu, Xin, Wilkinson, Martin, Cronin, Nora B., Dillingham, Mark S., Wigley, Dale B.
Format:	Journal Article
Language:	English
Published:	London Nature Publishing Group UK 17.04.2014 Nature Publishing Group
Subjects:	631/337/1427/2190 631/337/149 631/535/1266 Adenosine Triphosphate - analogs & derivatives Adenosine Triphosphate - metabolism Bacillus subtilis - enzymology Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Binding sites (Biochemistry) Crystallography, X-Ray DNA - chemistry DNA - genetics DNA - metabolism DNA Helicases - chemistry DNA Helicases - metabolism Exodeoxyribonucleases - chemistry Exodeoxyribonucleases - metabolism Genetic research Helicases Humanities and Social Sciences letter Models, Molecular Molecular Conformation multidisciplinary Proteins Recombination, Genetic - genetics Science Structure Structure-Activity Relationship Translocation (Genetics) United States
ISSN:	0028-0836, 1476-4687, 1476-4687
Online Access:	Get full text
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