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X-ray structure of a bacterial oligosaccharyltransferase

Author

Listed:
  • Christian Lizak

    (Institute of Microbiology, ETH Zurich
    Institute of Molecular Biology and Biophysics, ETH Zurich)

  • Sabina Gerber

    (Institute of Molecular Biology and Biophysics, ETH Zurich)

  • Shin Numao

    (Institute of Microbiology, ETH Zurich
    Present address: Novartis Pharma AG, CH-4002 Basel, Switzerland.)

  • Markus Aebi

    (Institute of Microbiology, ETH Zurich)

  • Kaspar P. Locher

    (Institute of Molecular Biology and Biophysics, ETH Zurich)

Abstract

Asparagine-linked glycosylation is a post-translational modification of proteins containing the conserved sequence motif Asn-X-Ser/Thr. The attachment of oligosaccharides is implicated in diverse processes such as protein folding and quality control, organism development or host–pathogen interactions. The reaction is catalysed by oligosaccharyltransferase (OST), a membrane protein complex located in the endoplasmic reticulum. The central, catalytic enzyme of OST is the STT3 subunit, which has homologues in bacteria and archaea. Here we report the X-ray structure of a bacterial OST, the PglB protein of Campylobacter lari, in complex with an acceptor peptide. The structure defines the fold of STT3 proteins and provides insight into glycosylation sequon recognition and amide nitrogen activation, both of which are prerequisites for the formation of the N-glycosidic linkage. We also identified and validated catalytically important, acidic amino acid residues. Our results provide the molecular basis for understanding the mechanism of N-linked glycosylation.

Suggested Citation

  • Christian Lizak & Sabina Gerber & Shin Numao & Markus Aebi & Kaspar P. Locher, 2011. "X-ray structure of a bacterial oligosaccharyltransferase," Nature, Nature, vol. 474(7351), pages 350-355, June.
    • Handle: RePEc:nat:nature:v:474:y:2011:i:7351:d:10.1038_nature10151
    DOI: 10.1038/nature10151
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    Cited by:

    1. Ana S. Ramírez & Mario Capitani & Giorgio Pesciullesi & Julia Kowal & Joël S. Bloch & Rossitza N. Irobalieva & Jean-Louis Reymond & Markus Aebi & Kaspar P. Locher, 2022. "Molecular basis for glycan recognition and reaction priming of eukaryotic oligosaccharyltransferase," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Beatriz Piniello & Javier Macías-León & Shun Miyazaki & Ana García-García & Ismael Compañón & Mattia Ghirardello & Víctor Taleb & Billy Veloz & Francisco Corzana & Atsushi Miyagawa & Carme Rovira & Ra, 2023. "Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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