Monomeric solution structure of the helicase binding domain of Escherichia coli DnaG primaseFaculty of Science, Medicine and Health - Papers
AbstractDnaG 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 InformationXun-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/