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Article
Monomeric solution structure of the helicase binding domain of Escherichia coli DnaG primase
Faculty of Science, Medicine and Health - Papers
  • Xun-Cheng Su, Australian National University
  • Patrick M Schaeffer, Australian National University
  • Karin V Loscha, Australian National University
  • Pamela H.P Gan, Australian National University
  • Nicholas E Dixon, University of Wollongong
  • Gottfried Otting, Australian National University
RIS ID
16850
Publication Date
1-1-2006
Publication Details

Su, X. Cheng., Schaeffer, P. M., Loscha, K., Gan, P. H.P., Dixon, N. E. & Otting, G. (2006). Monomeric solution structure of the helicase binding domain of Escherichia coli DnaG primase. The FEBS Journal, 273 (21), 4997-5009.

Abstract

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 absent in DnaB, as evidenced by high mobility of the C-terminal 35 residues in a construct comprising residues 1–171. The present structure identifies the previous crystal structure of the E. coli DnaG C-terminal domain as a domain-swapped dimer. It is also significantly different from the NMR structure reported for the corresponding domain of DnaG from the thermophile Bacillus stearothermophilus. NMR experiments showed that the DnaG C-terminal domain does not bind to residues 1–171 of the E. coli DnaB helicase with significant affinity.

Citation Information
Xun-Cheng Su, Patrick M Schaeffer, Karin V Loscha, Pamela H.P Gan, et al.. "Monomeric solution structure of the helicase binding domain of Escherichia coli DnaG primase" (2006)
Available at: http://works.bepress.com/nick_dixon/7/