ArticlePloS one2009
Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 34 citations in OpenAlex.
- Sequence-assignment validation in protein crystal structure models with checkMySequence.Acta crystallographica. Section D, Structural biology · 2023Article
- Diverse Mechanisms of Helicase Loading during DNA Replication Initiation in Bacteria.Journal of bacteriology · 2023Review
- Targeted chromosomal Escherichia coli:dnaB exterior surface residues regulate DNA helicase behavior to maintain genomic stability and organismal fitness.PLoS genetics · 2021Article
- Article
- Segmental isotope labelling and solid-state NMR of a 12 × 59 kDa motor protein: identification of structural variability.Journal of biomolecular NMR · 2018Article
- Screening of E. coli β-clamp Inhibitors Revealed that Few Inhibit Helicobacter pylori More Effectively: Structural and Functional Characterization.Antibiotics (Basel, Switzerland) · 2018Article
- DnaC, the indispensable companion of DnaB helicase, controls the accessibility of DnaB helicase by primase.The Journal of biological chemistry · 2017Article
- Structural insight into β-Clamp and its interaction with DNA Ligase in Helicobacter pylori.Scientific reports · 2016Article
- Variability and conservation of structural domains in divide-and-conquer approaches.Journal of biomolecular NMR · 2016Article
- 'Modulation of the enzymatic activities of replicative helicase (DnaB) by interaction with Hp0897: a possible mechanism for helicase loading in Helicobacter pylori'.Nucleic acids research · 2016Article
- Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.Journal of biomolecular NMR · 2016Article
- Structure and primase-mediated activation of a bacterial dodecameric replicative helicase.Nucleic acids research · 2015Article
- Genomics Analysis of Replicative Helicase DnaB Sequences in Proteobacteria.Acta informatica medica : AIM : journal of the Society for Medical Informatics of Bosnia & Herzegovina : casopis Drustva za medicinsku informatiku BiH · 2014Article
- Intracellular locations of replication proteins and the origin of replication during chromosome duplication in the slowly growing human pathogen Helicobacter pylori.Journal of bacteriology · 2014Article
- Nucleotide and partner-protein control of bacterial replicative helicase structure and function.Molecular cell · 2013Article
- Crystal structure and mode of helicase binding of the C-terminal domain of primase from Helicobacter pylori.Journal of bacteriology · 2013Article
- Class-specific restrictions define primase interactions with DNA template and replicative helicase.Nucleic acids research · 2010Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Replication initiation is a crucial step in genome duplication and homohexameric DnaB helicase plays a central role in the replication initiation process by unwinding the duplex DNA and interacting with several other proteins during the process of replication. N-terminal domain of DnaB is critical for helicase activity and for DnaG primase interactions. We present here the crystal structure of the N-terminal domain (NTD) of H. pylori DnaB (HpDnaB) helicase at 2.2 A resolution and compare the structural differences among helicases and correlate with the functional differences. The structural details of NTD suggest that the linker region between NTD and C-terminal helicase domain plays a vital role in accurate assembly of NTD dimers. The sequence analysis of the linker regions from several helicases reveals that they should form four helix bundles. We also report the characterization of H. pylori DnaG primase and study the helicase-primase interactions, where HpDnaG primase stimulates DNA unwinding activity of HpDnaB suggesting presence of helicase-primase cohort at the replication fork. The protein-protein interaction study of C-terminal domain of primase and different deletion constructs of helicase suggests that linker is essential for proper conformation of NTD to interact strongly with HpDnaG. The surface charge distribution on the primase binding surface of NTDs of various helicases suggests that DnaB-DnaG interaction and stability of the complex is most probably charge dependent. Structure of the linker and helicase-primase interactions indicate that HpDnaB differs greatly from E.coli DnaB despite both belong to gram negative bacteria.
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