TL;DR
The structure of the prototypical flagellum, including the basal body, export apparatus, motor complex, and extracellular hook-filament assembly, is reviewed, derived from recent cryo-EM studies.
Exploring bacteriophage structural diversity is essential for understanding phage biology and for advancing phage-based therapies. Here, we determine the cryo-electron microscopy structure of Jabs, providing, to our knowledge, the first high-resolution view of a phage infecting the multidrug-resistant human pathogen My...
Bacteriophage P2 is a long-standing model for contractile injection systems, yet high-resolution structures of the intact virion and the mechanism of baseplate activation have remained unresolved. Here, we combine high-resolution cryo-electron microscopy and in situ cryo-electron tomography to characterize P2, using it...
In-situ near-atomic structures of the sheathed flagellar motor within intact cells are determined, revealing how the distinctive architecture and dynamics of the sheathed flagellum support V. cholerae motility, environmental survival, and persistent colonization of the human gut.
Analysis of oligomeric organization and structural plasticity of the periplasmic domain of polar-flagellum FliL from Vibrio alginolyticus and compared with detergent-solubilized full-length pofFliL suggests that such plasticity enables FliL to act as an adaptable scaffold for stator engagement and mechanosensitive remo...
These findings provide the first molecular framework for understanding the organisation and assembly of the Clostridium spore envelope and reveal previously unrecognised principles governing the evolution of protective proteinaceous structures across the Bacillota (Firmicutes).
This study investigates the eukaryotic chaperonin CCT, a ~1 MDa hetero-oligomeric complex essential for the folding of key substrates such as actin, tubulin, and WD40 family members and demonstrates that subunit assignment and atomic modeling are achievable by exploiting subunit-intrinsic structural features alone.
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