Journal of Molecular Biology
CommunicationThe HexamericE. coliDnaB Helicase can Exist in Different Quarternary States
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DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase
2017, Journal of Biological ChemistryThe E. coli DNA Replication Fork
2016, EnzymesLoading strategies of ring-shaped nucleic acid translocases and helicases
2014, Current Opinion in Structural BiologyCitation Excerpt :DnaB-family proteins serve as central replicative helicases of bacteria (reviewed in [49]). Structural studies, including both EM and X-ray crystallography, have shown that DnaB orthologs readily form stable, closed hexameric rings [50–58]. In higher-resolution crystal structures, DnaB-family helicases have been found to adopt a two-tiered architecture, whereby a set of N-terminal primase interaction domains form a trimer of dimers that sits atop a pseudo-six-fold symmetric ring of RecA-type ATPase domains [53–55].
Nucleotide and partner-protein control of bacterial replicative helicase structure and function
2013, Molecular CellCitation Excerpt :Upon binding of ssDNA and nucleotide, however, the active sites of DnaB have recently been shown to condense into a more uniform, compact conformation that resembles related nucleotide-bound, hexameric helicases such as the Rho transcription termination factor and T7 bacteriophage gp4 (Itsathitphaisarn et al., 2012; Singleton et al., 2000; Thomsen and Berger, 2009). Interestingly, EM experiments have indicated that conformational heterogeneity persists within DnaB even when nucleotide is present, implying that the fully liganded helicase still exhibits significant plasticity (Yang et al., 2002; Yu et al., 1996). To better define the physical consequences of nucleotide binding to DnaB, we determined the crystal structure of the full-length helicase from A. aeolicus.
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