ArticleNucleic acids research2016
Taking a molecular motor for a spin: helicase mechanism studied by spin labeling and PELDOR.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Pulse dipolar EPR for determining nanomolar binding affinities.Chemical communications (Cambridge, England) · 2022Article
- Spin Labeling of Long RNAs Via Click Reaction and Enzymatic Ligation.Methods in molecular biology (Clifton, N.J.) · 2022Article
- PELDOR Measurements on Nitroxide-Labeled Oligonucleotides.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Nanomolar Pulse Dipolar EPR Spectroscopy in Proteins: CuThe journal of physical chemistry. B · 2021Article
- KERA: analysis tool for multi-process, multi-state single-molecule data.Nucleic acids research · 2021Article
- The contribution of modern EPR to structural biology.Emerging topics in life sciences · 2018Article
- Coherent pump pulses in Double Electron Electron Resonance spectroscopy.Physical chemistry chemical physics : PCCP · 2016Article
- Mechanism of DNA loading by the DNA repair helicase XPD.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The complex molecular motions central to the functions of helicases have long attracted attention. Protein crystallography has provided transformative insights into these dynamic conformational changes, however important questions about the true nature of helicase configurations during the catalytic cycle remain. Using pulsed EPR (PELDOR or DEER) to measure interdomain distances in solution, we have examined two representative helicases: PcrA from superfamily 1 and XPD from superfamily 2. The data show that PcrA is a dynamic structure with domain movements that correlate with particular functional states, confirming and extending the information gleaned from crystal structures and other techniques. XPD in contrast is shown to be a rigid protein with almost no conformational changes resulting from nucleotide or DNA binding, which is well described by static crystal structures. Our results highlight the complimentary nature of PELDOR to crystallography and the power of its precision in understanding the conformational changes relevant to helicase function.
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Registered trials
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