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A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader

Loscha, Karin; Jaudzems, Kristaps; Ioannou, Charikleia; Su, Xun-Cheng; Hill, Flynn R; Dixon, Nicholas; Liepinsh, Edvards; Otting, Gottfried

Description

The helicase loader protein DnaI (the Bacillus subtilis homologue of Escherichia coli DnaC) is required to load the hexameric helicase DnaC (the B. subtilis homologue of E. coli DnaB) onto DNA at the start of replication. While the C-terminal domain of DnaI belongs to the structurally well-characterized AAA+ family of ATPases, the structure of the N-terminal domain, DnaI-N, has no homology to a known structure. Three-dimensional structure determination by nuclear magnetic resonance (NMR)...[Show more]

CollectionsANU Research Publications
Date published: 2009-03-02
Type: Journal article
URI: http://hdl.handle.net/10440/540
http://digitalcollections.anu.edu.au/handle/10440/540
Source: Nucleic Acids Research
DOI: 10.1093/nar/gkp092

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