|Entry||Database: EMDB / ID: EMD-0397|
|Title||Cryo-EM reconstruction of Sulfolobus islandicus LAL14/1 Pilus|
|Sample||Sulfolobus islandicus LAL14/1 Pilus:|
|Function / homology||integral component of membrane / Uncharacterized protein|
Function and homology information
|Biological species||Sulfolobus islandicus LAL14/1 (acidophilic)|
|Method||helical reconstruction / cryo EM / Resolution: 4.1 Å|
|Authors||Wang F / Cvirkaite-Krupovic V / Prangishvili D / Krupovic M / Egelman EH|
|Funding support|| United States, 1 items |
|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.
|Validation Report||PDB-ID: 6nav|
SummaryFull reportAbout validation report
|Structure viewer||EM map: |
Downloads & links
|File||Download / File: emd_0397.map.gz / Format: CCP4 / Size: 216 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.4 Å|
|Symmetry||Space group: 1|
CCP4 map header:
-Entire Sulfolobus islandicus LAL14/1 Pilus
|Entire||Name: Sulfolobus islandicus LAL14/1 Pilus / Number of components: 2|
-Component #1: protein, Sulfolobus islandicus LAL14/1 Pilus
|Protein||Name: Sulfolobus islandicus LAL14/1 Pilus / Recombinant expression: No|
|Source||Species: Sulfolobus islandicus LAL14/1 (acidophilic)|
-Component #2: protein, M9UD72
|Protein||Name: M9UD72 / Number of Copies: 21 / Recombinant expression: No|
|Mass||Theoretical: 12.681375 kDa|
|Source||Species: Sulfolobus islandicus LAL14/1 (acidophilic)|
|Specimen||Specimen state: Filament / Method: cryo EM|
|Helical parameters||Axial symmetry: C1 (asymmetric) / Delta z: 4.94 Å / Delta phi: 104.97 %deg;|
|Sample solution||pH: 6|
|Vitrification||Cryogen name: ETHANE / Humidity: 90 %|
-Electron microscopy imaging
Model: Titan Krios / Image courtesy: FEI Company
|Imaging||Microscope: FEI TITAN KRIOS|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 48 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Imaging mode: BRIGHT FIELD|
|Specimen Holder||Model: OTHER|
|Camera||Detector: FEI FALCON III (4k x 4k)|
|Image acquisition||Details: Images were stored containing 24 fractions, where each fraction corresponded to a dose of ~2 electrons per Angstrom^2.|
|Processing||Method: helical reconstruction|
|3D reconstruction||Software: SPIDER, RELION / Resolution: 4.1 Å / Resolution method: OTHER / Details: MODEL:MAP FSC, D99|
-Atomic model buiding
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