6NAV
Cryo-EM reconstruction of Sulfolobus islandicus LAL14/1 Pilus
6NAV の概要
| エントリーDOI | 10.2210/pdb6nav/pdb |
| EMDBエントリー | 0397 |
| 分子名称 | M9UD72 (1 entity in total) |
| 機能のキーワード | helical symmetry, archaeal pilus, structural protein |
| 由来する生物種 | Sulfolobus islandicus LAL14/1 |
| タンパク質・核酸の鎖数 | 21 |
| 化学式量合計 | 266308.88 |
| 構造登録者 | Wang, F.,Cvirkaite-Krupovic, V.,Prangishvili, D.,Krupovic, M.,Egelman, E.H. (登録日: 2018-12-06, 公開日: 2019-05-08, 最終更新日: 2024-03-20) |
| 主引用文献 | Wang, F.,Cvirkaite-Krupovic, V.,Kreutzberger, M.A.B.,Su, Z.,de Oliveira, G.A.P.,Osinski, T.,Sherman, N.,DiMaio, F.,Wall, J.S.,Prangishvili, D.,Krupovic, M.,Egelman, E.H. An extensively glycosylated archaeal pilus survives extreme conditions. Nat Microbiol, 4:1401-1410, 2019 PubMed 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. PubMed: 31110358DOI: 10.1038/s41564-019-0458-x 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (4.1 Å) |
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