1jwe
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(New page: 200px<br /><applet load="1jwe" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jwe" /> '''NMR Structure of the N-Terminal Domain of E....)
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Revision as of 16:31, 20 November 2007
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NMR Structure of the N-Terminal Domain of E. Coli Dnab Helicase
Overview
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, 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.
About this Structure
1JWE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer., Weigelt J, Brown SE, Miles CS, Dixon NE, Otting G, Structure. 1999 Jun 15;7(6):681-90. PMID:10404597
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