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  • Title: Loading a ring: structure of the Bacillus subtilis DnaB protein, a co-loader of the replicative helicase.
    Author: Núñez-Ramírez R, Velten M, Rivas G, Polard P, Carazo JM, Donate LE.
    Journal: J Mol Biol; 2007 Mar 30; 367(3):764-9. PubMed ID: 17289076.
    Abstract:
    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.
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