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Solution structure of Domains IVa and V of the τ subunit of Escherichia coli DNA polymerase III and interaction with the α subunit

Su, Xun-Cheng; Jergic, Slobodan; Keniry, Max; Dixon, Nicholas; Otting, Gottfried


The solution structure of the C-terminal Domain V of the τ subunit of E. coli DNA polymerase III was determined by nuclear magnetic resonance (NMR) spectroscopy. The fold is unique to τ subunits. Amino acid sequence conservation is pronounced for hydrophobic residues that form the structural core of the protein, indicating that the fold is representative for τ subunits from a wide range of different bacteria. The interaction between the polymerase subunits τ and α was studied by NMR...[Show more]

CollectionsANU Research Publications
Date published: 2007-04-22
Type: Journal article
Source: Nucleic Acids Research
DOI: 10.1093/nar/gkm080


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