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New page: left|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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[[Image:1jwe.gif|left|200px]]<br /><applet load="1jwe" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1jwe.gif|left|200px]]<br /><applet load="1jwe" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1jwe" />
caption="1jwe" />
'''NMR Structure of the N-Terminal Domain of E. Coli Dnab Helicase'''<br />
'''NMR Structure of the N-Terminal Domain of E. Coli Dnab Helicase'''<br />


==Overview==
==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.
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==
==About this Structure==
1JWE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JWE OCA].  
1JWE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWE OCA].  


==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Brown, S.E.]]
[[Category: Brown, S E.]]
[[Category: Dixon, N.E.]]
[[Category: Dixon, N E.]]
[[Category: Miles, C.S.]]
[[Category: Miles, C S.]]
[[Category: Otting, G.]]
[[Category: Otting, G.]]
[[Category: Weigelt, J.]]
[[Category: Weigelt, J.]]
[[Category: helicase]]
[[Category: helicase]]


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