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Crystal and solution structures of the helicase-binding domain of Escherichia coli primase

Oakley, Aaron; Loscha, Karin; Schaeffer, Patrick; Liepinsh, Edvards; Pintacuda, Guido; Wilce, Matthew; Otting, Gottfried; Dixon, Nicholas

Description

During bacterial DNA replication, the DnaG primase interacts with the hexameric DnaB helicase to synthesize RNA primers for extension by DNA polymerase. In Escherichia coli, this occurs by transient interaction of primase with the helicase. Here we demonstrate directly by surface plasmon resonance that the C-terminal domain of primase is responsible for interaction with DnaB6. Determination of the 2.8-Å crystal structure of the C-terminal domain of primase revealed an asymmetric dimer. The...[Show more]

CollectionsANU Research Publications
Date published: 2005
Type: Journal article
URI: http://hdl.handle.net/1885/76087
Source: Journal of Biological Chemistry
DOI: 10.1074/jbc.M412645200

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