3BGW

The Structure Of A DnaB-Like Replicative Helicase And Its Interactions With Primase

Summary for 3BGW

• Entry DOI: 10.2210/pdb3bgw/pdb
• Related: 3BHO
• Descriptor: DNAB-Like Replicative Helicase (1 entity in total)
• Functional Keywords: atpase, replication
• Biological source: Bacillus phage SPP1
• Total number of polymer chains: 6
• Total formula weight: 300085.62

Authors

Wang, G.,Klein, M.G.,Tokonzaba, E.,Zhang, Y.,Holden, L.G.,Chen, X.S. (deposition date: 2007-11-27, release date: 2007-12-25, Last modification date: 2024-10-09)

Primary citation

Wang, G.,Klein, M.G.,Tokonzaba, E.,Zhang, Y.,Holden, L.G.,Chen, X.S.
The structure of a DnaB-family replicative helicase and its interactions with primase.
Nat.Struct.Mol.Biol., 15:94-100, 2008

PubMed Abstract: Helicases are essential enzymes for DNA replication, a fundamental process in all living organisms. The DnaB family are hexameric replicative helicases that unwind duplex DNA and coordinate with RNA primase and other proteins at the replication fork in prokaryotes. Here, we report the full-length crystal structure of G40P, a DnaB family helicase. The hexamer complex reveals an unusual architectural feature and a new type of assembly mechanism. The hexamer has two tiers: a three-fold symmetric N-terminal tier and a six-fold symmetric C-terminal tier. Monomers with two different conformations, termed cis and trans, come together to provide a topological solution for the dual symmetry within a hexamer. Structure-guided mutational studies indicate an important role for the N-terminal tier in binding primase and regulating primase-mediated stimulation of helicase activity. This study provides insights into the structural and functional interplay between G40P helicase and DnaG primase.

PubMed: 18157148
DOI: 10.1038/nsmb1356

Experimental method

X-RAY DIFFRACTION (3.91 Å)