ArticleJournal of biomolecular NMR2016
Solid-state NMR chemical-shift perturbations indicate domain reorientation of the DnaG primase in the primosome of Helicobacter pylori.
Article in Journal of biomolecular NMR, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Co-sedimentation is the key to the structural investigation of wild-type FAT10.Journal of biomolecular NMR · 2026Article
- Intermolecular β-sheet Formation Guides the Interaction between Ubiquitin-like Modifier FAT10 and Adapter Protein NUB1L.Journal of the American Chemical Society · 2026Article
- Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.Nature communications · 2021Article
- Paramagnetic Solid-State NMR to Localize the Metal-Ion Cofactor in an Oligomeric DnaB Helicase.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021Article
- Characterization of nucleosome sediments for protein interaction studies by solid-state NMR spectroscopy.Magnetic resonance (Gottingen, Germany) · 2021Article
- ATP Analogues for Structural Investigations: Case Studies of a DnaB Helicase and an ABC Transporter.Molecules (Basel, Switzerland) · 2020Review
- Sedimentation Yields Long-Term Stable Protein Samples as Shown by Solid-State NMR.Frontiers in molecular biosciences · 2020Article
- Simple high-resolution NMR spectroscopy as a tool in molecular biology.The FEBS journal · 2019Article
- The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase.Nature communications · 2019Article
- Variability and conservation of structural domains in divide-and-conquer approaches.Journal of biomolecular NMR · 2016Article
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We here investigate the interactions between the DnaB helicase and the C-terminal domain of the corresponding DnaG primase of Helicobacter pylori using solid-state NMR. The difficult crystallization of this 387 kDa complex, where the two proteins interact in a six to three ratio, is circumvented by simple co-sedimentation of the two proteins directly into the MAS-NMR rotor. While the amount of information that can be extracted from such a large protein is still limited, we can assign a number of amino-acid residues experiencing significant chemical-shift perturbations upon helicase-primase complex formation. The location of these residues is used as a guide to model the interaction interface between the two proteins in the complex. Chemical-shift perturbations also reveal changes at the interaction interfaces of the hexameric HpDnaB assembly on HpDnaG binding. A structural model of the complex that explains the experimental findings is obtained.
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