PMID:10404598

Citation	Fass, D, Bogden, CE and Berger, JM (1999) Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 7:691-8
Abstract	The hexameric helicase DnaB unwinds the DNA duplex at the Escherichia coli chromosome replication fork. Although the mechanism by which DnaB both couples ATP hydrolysis to translocation along DNA and denatures the duplex is unknown, a change in the quaternary structure of the protein involving dimerization of the N-terminal domain has been observed and may occur during the enzymatic cycle. This N-terminal domain is required both for interaction with other proteins in the primosome and for DnaB helicase activity. Knowledge of the structure of this domain may contribute to an understanding of its role in DnaB function.
Links	PubMed
Keywords	Adenosine Triphosphatases/chemistry; Amino Acid Sequence; Bacterial Proteins; Crystallography, X-Ray; DNA Helicases/chemistry; Dimerization; DnaB Helicases; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Peptide Fragments/chemistry; Protein Conformation; Protein Folding; Protein Structure, Secondary
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