The DnaB.DnaC complex: a structure based on dimers assembled around an occluded channel.

@article{Barcena2001TheDC,
  title={The DnaB.DnaC complex: a structure based on dimers assembled around an occluded channel.},
  author={Martin Barcena and Teresa Ruiz and Luis Enrique Donate and Suzanne E. Brown and Nicholas E Dixon and Michael Radermacher and Jos{\'e} Mar{\'i}a Carazo},
  journal={The EMBO journal},
  year={2001},
  volume={20 6},
  pages={1462-8}
}
Replicative helicases are motor proteins that unwind DNA at replication forks. Escherichia coli DnaB is the best characterized member of this family of enzymes. We present the 26 A resolution three-dimensional structure of the DnaB hexamer in complex with its loading partner, DnaC, obtained from cryo-electron microscopy. Analysis of the volume brings insight into the elaborate way the two proteins interact, and provides a structural basis for control of the symmetry state and inactivation of… CONTINUE READING