An extensively glycosylated archaeal pilus survives extreme conditions View Full Text


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Article Info

DATE

2019-05-20

AUTHORS

Fengbin Wang, Virginija Cvirkaite-Krupovic, Mark A.B. Kreutzberger, Zhangli Su, Guilherme A.P. de Oliveira, Tomasz Osinski, Nicholas Sherman, Frank DiMaio, Joseph S. Wall, David Prangishvili, Mart Krupovic, Edward H. Egelman

ABSTRACT

Pili on the surface of Sulfolobus islandicus are used for many functions, and serve as receptors for certain archaeal viruses. The cells grow optimally at pH 3 and ~80 °C, exposing these extracellular appendages to a very harsh environment. The pili, when removed from cells, resist digestion by trypsin or pepsin, and survive boiling in sodium dodecyl sulfate or 5 M guanidine hydrochloride. We used electron cryo-microscopy to determine the structure of these filaments at 4.1 Å resolution. An atomic model was built by combining the electron density map with bioinformatics without previous knowledge of the pilin sequence-an approach that should prove useful for assemblies where all of the components are not known. The atomic structure of the pilus was unusual, with almost one-third of the residues being either threonine or serine, and with many hydrophobic surface residues. While the map showed extra density consistent with glycosylation for only three residues, mass measurements suggested extensive glycosylation. We propose that this extensive glycosylation renders these filaments soluble and provides the remarkable structural stability. We also show that the overall fold of the archaeal pilin is remarkably similar to that of archaeal flagellin, establishing common evolutionary origins. More... »

PAGES

1401-1410

References to SciGraph publications

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  • 2015-02-23. Atomic accuracy models from 4.5 Å cryo-electron microscopy data with density-guided iterative local refinement in NATURE METHODS
  • 2017-10-09. Structure of the calcium dependent type 2 secretion pseudopilus in NATURE MICROBIOLOGY
  • 2015-02-23. De novo protein structure determination from near-atomic resolution cryo-EM maps in NATURE METHODS
  • 2017-11-10. Unique architecture of thermophilic archaeal virus APBV1 and its genome packaging in NATURE COMMUNICATIONS
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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41564-019-0458-x

    DOI

    http://dx.doi.org/10.1038/s41564-019-0458-x

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1114910165

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/31110358


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    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/pub.10.1038/s41564-019-0458-x'

    RDF/XML is a standard XML format for linked data.

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/pub.10.1038/s41564-019-0458-x'


     

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