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Showing 1–9 of 9 results
Advanced filters: Author: Michail N. Isupov Clear advanced filters

  • The model archaeon Sulfolobus acidocaldarius produces several protein filaments with specialised functions, including flagellum-like archaella, Aap pili, and adhesive threads. Here, the authors describe high-resolution structures and distinct glycosylation patterns for the three filaments, and present an integrated model of the filaments in the context of the S-layer.

    • Matthew C. Gaines
    • Michail N. Isupov
    • Bertram Daum
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-16

  • The archaellum is a molecular machine used by archaea to swim, consisting of an intracellular motor that drives the rotation of an extracellular filament composed of multiple copies of proteins named archaellins. Here, the authors use electron cryo-microscopy to elucidate the structure of an archaellum, and find that the filament is composed of two alternating archaellins.

    • Lavinia Gambelli
    • Michail N. Isupov
    • Bertram Daum
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-11

  • Oxyanion stabilization is essential for E2 enzyme activity in ubiquitin and Ub-like protein conjugation. Here, the authors demonstrate that E2 enzymes (1) employ C-alpha hydrogen bonding for oxyanion stabilization and (2) feature an additional oxyanion hole that facilitates cis conjugation, together highlighting the adaptability of E2 enzymes.

    • Manoj Kumar
    • Sayanika Banerjee
    • Reuven Wiener
    ResearchOpen Access
    Nature Communications
    Volume: 16, P: 1-17

  • The cells of many archaeal species display surface appendages that closely resemble bacterial Type IV pili (T4P). Here, Gaines et al. present a cryoEM structure of the archaeal adhesive pilus from Sulfolobus acidocaldarius, showing that the structure of the component subunit follows the canonical T4P blueprint but adopts three distinct conformations within the pilus.

    • Matthew C. Gaines
    • Shamphavi Sivabalasarma
    • Bertram Daum
    ResearchOpen Access
    Nature Communications
    Volume: 15, P: 1-13

  • Pili are filamentous appendages on the surface of bacteria and archaea, and play roles in multiple processes such as adhesion, motility and horizontal gene transfer. Here, Gaines et al. describe the structure of a new type of pilus, termed ‘thread’, from the model archaeaon Sulfolobus acidocaldarius.

    • Matthew C. Gaines
    • Michail N. Isupov
    • Bertram Daum
    ResearchOpen Access
    Nature Communications
    Volume: 13, P: 1-13

  • Ufmylation is a well-established ubiquitin-like protein modification, but its mechanism is largely unclear. Here, the authors present a crystal structure of the ufmylation-specific E1-E2 complex, revealing differences to the ubiquitination machinery and mechanistic details of the ufmylation process.

    • Manoj Kumar
    • Prasanth Padala
    • Reuven Wiener
    ResearchOpen Access
    Nature Communications
    Volume: 12, P: 1-13