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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]

dc.contributor.authorSu, Xun-Cheng
dc.contributor.authorSchaeffer, Patrick
dc.contributor.authorLoscha, Karin
dc.contributor.authorGan, Pamela
dc.contributor.authorDixon, Nicholas
dc.contributor.authorOtting, Gottfried
dc.date.accessioned2015-12-07T22:27:56Z
dc.identifier.issn1742-464X
dc.identifier.urihttp://hdl.handle.net/1885/22133
dc.description.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.
dc.publisherBlackwell Publishing Ltd
dc.sourceThe FEBS Journal
dc.subjectKeywords: bacterial DNA; DNA primase; DnaG primase; helicase; primer RNA; single stranded DNA; unclassified drug; article; carboxy terminal sequence; crystal structure; DNA helix; DNA replication; Escherichia coli; Geobacillus stearothermophilus; nonhuman; nuclear DnaB; DnaG; Domain swap; NMR structure; Primase
dc.titleMonomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase.
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume273
dc.date.issued2006
local.identifier.absfor060199 - Biochemistry and Cell Biology not elsewhere classified
local.identifier.absfor060107 - Enzymes
local.identifier.ariespublicationu4217927xPUB20
local.type.statusPublished Version
local.contributor.affiliationSu, Xun-Cheng, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationSchaeffer, Patrick, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationLoscha, Karin, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationGan, Pamela, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationDixon, Nicholas, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationOtting, Gottfried, College of Physical and Mathematical Sciences, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue21
local.bibliographicCitation.startpage4997
local.bibliographicCitation.lastpage5009
local.identifier.doi10.1111/j.1742-4658.2006.05495.x
dc.date.updated2015-12-07T09:58:29Z
local.identifier.scopusID2-s2.0-33750055730
CollectionsANU Research Publications

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