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TitleLoading a ring: structure of the Bacillus subtilis DnaB protein, a co-loader of the replicative helicase.
Journal, issue, pagesJ Mol Biol, Vol. 367, Issue 3, Page 764-769, Year 2007
Publish dateMar 30, 2007
AuthorsRafael Núñez-Ramírez / Marion Velten / Germán Rivas / Patrice Polard / José María Carazo / Luis Enrique Donate /
PubMed AbstractLoading of the ring-shaped replicative helicase is a critical step in the initiation of DNA replication. Bacillus subtilis has adopted a two-protein strategy to load its hexameric replicative ...Loading of the ring-shaped replicative helicase is a critical step in the initiation of DNA replication. Bacillus subtilis has adopted a two-protein strategy to load its hexameric replicative helicase: DnaB and DnaI interact with the helicase and mediate its delivery onto DNA. We present here the 3D electron microscopy structure of the DnaB protein, along with a detailed analysis of both its oligomeric state and its domain organization. DnaB is organized as an asymmetric tetramer that is comprised of two stacked components, one arranged as a closed collar and the other as an open sigma shape. Intriguingly, the 3D map of DnaB exhibits an overall architecture similar to the structure of the Escherichia coli gamma-complex, the loader of the ring-shaped processivity factor. We propose a model whereby each DnaB monomer participates in both stacked components of the tetramer and displays a different overall shape. This asymmetric quaternary organization could be a general feature of ring loaders.
External linksJ Mol Biol / PubMed:17289076
MethodsEM (single particle)
Resolution24.0 Å
Structure data

EMDB-1225:
Loading a ring: structure of the Bacillus subtilis DnaB protein, a co-loader of the replicative helicase.
Method: EM (single particle) / Resolution: 24.0 Å

Source
  • Bacillus subtilis (bacteria)

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