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1jwe

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NMR Structure of the N-Terminal Domain of E. Coli Dnab Helicase

Structural highlights

1jwe is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DNAB_ECOLI Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Weigelt J, Brown SE, Miles CS, Dixon NE, Otting G. NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure. 1999 Jun 15;7(6):681-90. PMID:10404597

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jwe"

@@ Line 1: / Line 1: @@
 ==NMR Structure of the N-Terminal Domain of E. Coli Dnab Helicase==
-<StructureSection load='1jwe' size='340' side='right'caption='[[1jwe]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1jwe' size='340' side='right'caption='[[1jwe]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jwe]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JWE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jwe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JWE FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwe OCA], [http://pdbe.org/1jwe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jwe RCSB], [http://www.ebi.ac.uk/pdbsum/1jwe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwe ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jwe OCA], [https://pdbe.org/1jwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jwe RCSB], [https://www.ebi.ac.uk/pdbsum/1jwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jwe ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DNAB_ECOLI DNAB_ECOLI]] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
+[https://www.uniprot.org/uniprot/DNAB_ECOLI DNAB_ECOLI] Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
 [[Category: Large Structures]]
-[[Category: Brown, S E]]
+[[Category: Brown SE]]
-[[Category: Dixon, N E]]
+[[Category: Dixon NE]]
-[[Category: Miles, C S]]
+[[Category: Miles CS]]
-[[Category: Otting, G]]
+[[Category: Otting G]]
-[[Category: Weigelt, J]]
+[[Category: Weigelt J]]
-[[Category: Helicase]]
-[[Category: Hydrolase]]

1jwe

From Proteopedia

Current revision

NMR Structure of the N-Terminal Domain of E. Coli Dnab Helicase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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