4zc0 | pdb_00004zc0

Structure of a dodecameric bacterial helicase

spinqualitylabelsall models 4zc0, resolution 6.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4zc0 is a 4 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TBR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DNAB_HELPY Participates in initiation and elongation during chromosome replication; it exhibits DNA-dependent ATPase activity and contains distinct active sites for ATP binding, DNA binding, and interaction with DnaC protein, primase, and other prepriming proteins (By similarity). Publication Abstract from PubMed Replicative helicases are essential ATPases that unwind DNA to initiate chromosomal replication. While bacterial replicative DnaB helicases are hexameric, Helicobacter pylori DnaB (HpDnaB) was found to form double hexamers, similar to some archaeal and eukaryotic replicative helicases. Here we present a structural and functional analysis of HpDnaB protein during primosome formation. The crystal structure of the HpDnaB at 6.7 A resolution reveals a dodecameric organization consisting of two hexamers assembled via their N-terminal rings in a stack-twisted mode. Using fluorescence anisotropy we show that HpDnaB dodecamer interacts with single-stranded DNA in the presence of ATP but has a low DNA unwinding activity. Multi-angle light scattering and small angle X-ray scattering demonstrate that interaction with the DnaG primase helicase-binding domain dissociates the helicase dodecamer into single ringed primosomes. Functional assays on the proteins and associated complexes indicate that these single ringed primosomes are the most active form of the helicase for ATP hydrolysis, DNA binding and unwinding. These findings shed light onto an activation mechanism of HpDnaB by the primase that might be relevant in other bacteria and possibly other organisms exploiting dodecameric helicases for DNA replication. Structure and primase-mediated activation of a bacterial dodecameric replicative helicase.,Bazin A, Cherrier MV, Gutsche I, Timmins J, Terradot L Nucleic Acids Res. 2015 Sep 30;43(17):8564-76. doi: 10.1093/nar/gkv792. Epub 2015, Aug 11. PMID:26264665 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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