9ETU の概要
エントリーDOI | 10.2210/pdb9etu/pdb |
EMDBエントリー | 19962 |
分子名称 | Archaellin, 3-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-beta-D-glucopyranuronic acid-(1-4)-beta-D-glucopyranose (2 entities in total) |
機能のキーワード | archaellum, haloarcheon, archaellin, structural protein |
由来する生物種 | Halobacterium salinarum |
タンパク質・核酸の鎖数 | 25 |
化学式量合計 | 533322.68 |
構造登録者 | |
主引用文献 | Sofer, S.,Vershinin, Z.,Mashni, L.,Zalk, R.,Shahar, A.,Eichler, J.,Grossman-Haham, I. Perturbed N-glycosylation of Halobacterium salinarum archaellum filaments leads to filament bundling and compromised cell motility. Nat Commun, 15:5841-5841, 2024 Cited by PubMed Abstract: The swimming device of archaea-the archaellum-presents asparagine (N)-linked glycans. While N-glycosylation serves numerous roles in archaea, including enabling their survival in extreme environments, how this post-translational modification contributes to cell motility remains under-explored. Here, we report the cryo-EM structure of archaellum filaments from the haloarchaeon Halobacterium salinarum, where archaellins, the building blocks of the archaellum, are N-glycosylated, and the N-glycosylation pathway is well-resolved. We further determined structures of archaellum filaments from two N-glycosylation mutant strains that generate truncated glycans and analyzed their motility. While cells from the parent strain exhibited unidirectional motility, the N-glycosylation mutant strain cells swam in ever-changing directions within a limited area. Although these mutant strain cells presented archaellum filaments that were highly similar in architecture to those of the parent strain, N-linked glycan truncation greatly affected interactions between archaellum filaments, leading to dramatic clustering of both isolated and cell-attached filaments. We propose that the N-linked tetrasaccharides decorating archaellins act as physical spacers that minimize the archaellum filament aggregation that limits cell motility. PubMed: 38992036DOI: 10.1038/s41467-024-50277-1 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (3.33 Å) |
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