Ontology highlight
ABSTRACT:
SUBMITTER: Bailey S
PROVIDER: S-EPMC1950529 | biostudies-literature | 2007
REPOSITORIES: biostudies-literature
Bailey Scott S Eliason William K WK Steitz Thomas A TA
Nucleic acids research 20070701 14
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 A 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 ...[more]