|Entry||Database: PDB / ID: 6nav|
|Title||Cryo-EM reconstruction of Sulfolobus islandicus LAL14/1 Pilus|
|Keywords||STRUCTURAL PROTEIN / helical symmetry / archaeal pilus|
|Function / homology||integral component of membrane / Uncharacterized protein|
Function and homology information
|Biological species||Sulfolobus islandicus LAL14/1 (acidophilic)|
|Method||ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 4.1 Å|
|Authors||Wang, F. / Cvirkaite-Krupovic, V. / Prangishvili, D. / Krupovic, M. / Egelman, E.H.|
|Funding support|| United States, 1items |
|Citation||Journal: Nat Microbiol / Year: 2019|
Title: An extensively glycosylated archaeal pilus survives extreme conditions.
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 ...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 ...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.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
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Mass: 12681.375 Da / Num. of mol.: 21 / Source method: isolated from a natural source
Source: (natural) Sulfolobus islandicus LAL14/1 (acidophilic)
References: UniProt: M9UD72
|Experiment||Method: ELECTRON MICROSCOPY|
|EM experiment||Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction|
|Component||Name: Sulfolobus islandicus LAL14/1 Pilus / Type: COMPLEX / Entity ID: 1 / Source: NATURAL|
|Molecular weight||Experimental value: NO|
|Source (natural)||Organism: Sulfolobus islandicus LAL14/1 (acidophilic)|
|Buffer solution||pH: 6|
|Specimen||Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES|
|Vitrification||Cryogen name: ETHANE / Humidity: 90 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Microscopy||Model: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM|
|Electron lens||Mode: BRIGHT FIELDBright-field microscopy|
|Image recording||Average exposure time: 2 sec. / Electron dose: 48 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k)|
Details: Images were stored containing 24 fractions, where each fraction corresponded to a dose of ~2 electrons per Angstrom^2.
|Software||Name: PHENIX / Version: dev_2919: / Classification: refinement|
|CTF correction||Type: PHASE FLIPPING AND AMPLITUDE CORRECTION|
|Helical symmerty||Angular rotation/subunit: 104.97 ° / Axial rise/subunit: 4.94 Å / Axial symmetry: C1|
|3D reconstruction||Resolution: 4.1 Å / Resolution method: OTHER / Num. of particles: 181070 / Details: MODEL:MAP FSC, D99 / Symmetry type: HELICAL|
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