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Title: The Crystal Structure of the Thermus Aquaticus DnaB Helicase Monomer

Abstract

The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly dimer, at 2.9 {angstrom} resolution. DnaB is a highly flexible two domain protein. The C-terminal domain exhibits a RecA-like core fold and contains all the conserved sequence motifs that are characteristic of the DnaB helicase family. The N-terminal domain contains an additional helical hairpin that makes it larger than previously appreciated. Several DnaB mutations that modulate its interaction with primase are found in this hairpin. The similarity in the fold of the DnaB N-terminal domain with that of the C-terminal helicase-binding domain (HBD) of the DnaG primase also includes this hairpin. Comparison of hexameric homology models of DnaB with the structure of the papillomavirus E1 helicase suggests the two helicases may function through different mechanisms despite their sharing a common ancestor.

Authors:
; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930031
Report Number(s):
BNL-80647-2008-JA
Journal ID: ISSN 0305-1048; NARHAD; TRN: US200822%%1266
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Nucleic Acids Research; Journal Volume: 35
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; DNA; FUNCTIONS; INTERACTIONS; MONOMERS; MUTATIONS; RESOLUTION; national synchrotron light source

Citation Formats

Bailey,S., Eliason, W., and Steitz, T. The Crystal Structure of the Thermus Aquaticus DnaB Helicase Monomer. United States: N. p., 2007. Web. doi:10.1093/nar/gkm507.
Bailey,S., Eliason, W., & Steitz, T. The Crystal Structure of the Thermus Aquaticus DnaB Helicase Monomer. United States. doi:10.1093/nar/gkm507.
Bailey,S., Eliason, W., and Steitz, T. Mon . "The Crystal Structure of the Thermus Aquaticus DnaB Helicase Monomer". United States. doi:10.1093/nar/gkm507.
@article{osti_930031,
title = {The Crystal Structure of the Thermus Aquaticus DnaB Helicase Monomer},
author = {Bailey,S. and Eliason, W. and Steitz, T.},
abstractNote = {The ring-shaped hexameric DnaB helicase unwinds duplex DNA at the replication fork of eubacteria. We have solved the crystal structure of the full-length Thermus aquaticus DnaB monomer, or possibly dimer, at 2.9 {angstrom} resolution. DnaB is a highly flexible two domain protein. The C-terminal domain exhibits a RecA-like core fold and contains all the conserved sequence motifs that are characteristic of the DnaB helicase family. The N-terminal domain contains an additional helical hairpin that makes it larger than previously appreciated. Several DnaB mutations that modulate its interaction with primase are found in this hairpin. The similarity in the fold of the DnaB N-terminal domain with that of the C-terminal helicase-binding domain (HBD) of the DnaG primase also includes this hairpin. Comparison of hexameric homology models of DnaB with the structure of the papillomavirus E1 helicase suggests the two helicases may function through different mechanisms despite their sharing a common ancestor.},
doi = {10.1093/nar/gkm507},
journal = {Nucleic Acids Research},
number = ,
volume = 35,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}