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Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase.

Su, Xun-Cheng; Schaeffer, Patrick; Loscha, Karin; Gan, Pamela; Dixon, Nicholas; Otting, Gottfried

Description

DnaG is the primase that lays down RNA primers on single-stranded DNA during bacterial DNA replication. The solution structure of the DnaB-helicase-binding C-terminal domain of Escherichia coli DnaG was determined by NMR spectroscopy at near-neutral pH. The structure is a rare fold that, besides occurring in DnaG C-terminal domains, has been described only for the N-terminal domain of DnaB. The C-terminal helix hairpin present in the DnaG C-terminal domain, however, is either less stable or...[Show more]

CollectionsANU Research Publications
Date published: 2006
Type: Journal article
URI: http://hdl.handle.net/1885/22133
Source: The FEBS Journal
DOI: 10.1111/j.1742-4658.2006.05495.x

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