Summary for 9EQ7
| Entry DOI | 10.2210/pdb9eq7/pdb |
| EMDB information | 19905 |
| Descriptor | Archaellin, 2-O-sulfo-beta-D-glucopyranuronic acid-(1-4)-3-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-beta-D-glucopyranuronic acid-(1-4)-beta-D-glucopyranose (2 entities in total) |
| Functional Keywords | archaellum, haloarcheon, archaellin, structural protein |
| Biological source | Halobacterium salinarum |
| Total number of polymer chains | 26 |
| Total formula weight | 567977.31 |
| Authors | Grossman-Haham, I.,Shahar, A. (deposition date: 2024-03-21, release date: 2024-07-17, Last modification date: 2024-10-23) |
| Primary citation | 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 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.23 Å) |
Structure validation
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