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NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer

Weigelt, Johan; Brown, Susan Elizabeth; Miles, Caroline; Dixon, Nicholas; Otting, Gottfried

Description

Background: DnaB is the primary replicative helicase in Escherichia coli. Native DnaB is a hexamer of identical subunits, each consisting of a larger C-terminal domain and a smaller N-terminal domain. Electron-microscopy data show hexamers with C6 or C3 symmetry, indicating large domain movements and reversible pairwise association. Results: The three-dimensional structure of the N-terminal domain of E. coli DnaB was determined by nuclear magnetic resonance (NMR) spectroscopy. Structural...[Show more]

dc.contributor.authorWeigelt, Johan
dc.contributor.authorBrown, Susan Elizabeth
dc.contributor.authorMiles, Caroline
dc.contributor.authorDixon, Nicholas
dc.contributor.authorOtting, Gottfried
dc.date.accessioned2015-12-13T23:35:18Z
dc.identifier.issn0969-2126
dc.identifier.urihttp://hdl.handle.net/1885/93858
dc.description.abstractBackground: DnaB is the primary replicative helicase in Escherichia coli. Native DnaB is a hexamer of identical subunits, each consisting of a larger C-terminal domain and a smaller N-terminal domain. Electron-microscopy data show hexamers with C6 or C3 symmetry, indicating large domain movements and reversible pairwise association. Results: The three-dimensional structure of the N-terminal domain of E. coli DnaB was determined by nuclear magnetic resonance (NMR) spectroscopy. Structural similarity was found with the primary dimerisation domain of a topoisomerase, the gyrase A subunit from E. coli. A monomer-dimer equilibrium was observed for the isolated N-terminal domain of DnaB. A dimer model with C2 symmetry was derived from intermolecular nuclear Overhauser effects, which is consistent with all available NMR data. Conclusions: The monomer-dimer equilibrium observed for the N-terminal domain of DnaB is likely to be of functional significance for helicase activity, by participating in the switch between C6 and C3 symmetry of the helicase hexamer.
dc.publisherCell Press
dc.sourceStructure
dc.subjectKeywords: DNA b; helicase; amino acid sequence; amino terminal sequence; article; dimerization; enzyme activity; enzyme structure; escherichia coli; nonhuman; nuclear magnetic resonance imaging; nucleotide sequence; priority journal; protein domain; structure analy DnaB; Helicase; NMR
dc.titleNMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume7
dc.date.issued1999
local.identifier.absfor030505 - Physical Organic Chemistry
local.identifier.ariespublicationMigratedxPub25280
local.type.statusPublished Version
local.contributor.affiliationWeigelt, Johan, Karolinska Institutet
local.contributor.affiliationBrown, Susan Elizabeth, College of Physical and Mathematical Sciences, ANU
local.contributor.affiliationMiles, Caroline, 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.startpage681?690
local.identifier.doi10.1016/S0969-2126(99)80089-6
dc.date.updated2015-12-12T09:39:28Z
local.identifier.scopusID2-s2.0-1542563746
CollectionsANU Research Publications

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