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Showing 1–4 of 4 results
Advanced filters: Author: Jana Škerlová Clear advanced filters

  • Using cryo-electron microscopy technologies, Serianni and Škerlová et al. reveal how NpnNs initiate bacterial transcription as noncanonical RNA caps by showing one nucleobase pairing with the template in canonical mode while the other pairs in reverse Watson–Crick mode.

    • Valentina M. Serianni
    • Jana Škerlová
    • Hana Cahova
    ResearchOpen Access
    Nature Chemical Biology
    P: 1-8

  • The pyruvate dehydrogenase complex (PDHc) is a large multienzyme complex that converts pyruvate into acetyl-coenzyme A and in E. coli the core of the PDHc is formed by 24 copies of dihydrolipoyl transacetylase. Here, the authors present the cryo-EM structure of the E. coli dihydrolipoyl transacetylase 24-mer core in a native resting state including lipoyl domains, and discuss the mechanism of substrate shuttling by the lipoyl domains.

    • Jana Škerlová
    • Jens Berndtsson
    • Pål Stenmark
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-10

  • Botulinum neurotoxins (BoNTs) are a family of protein toxins produced by clostridial bacteria that cause muscle paralysis, and exhibit structural and functional diversity within the BoNTs family. Here, the authors report the cryo-EM structure complex of a newly identified serotype BoNT/X with their partner protein NTNH/X and reveal the complex’s pH-dependent stability and receptor-binding properties.

    • Markel Martínez-Carranza
    • Jana Škerlová
    • Pål Stenmark
    ResearchOpen Access
    Communications Chemistry
    Volume: 7, P: 1-15