The University of Osaka · Biochemistry, Genetics and Molecular Biology
Professor Takayuki Kato's research lab specializes in structural biology, with a focus on high-resolution cryo-electron microscopy (cryoEM) to unravel the atomic-level architecture of complex biological nanostructures. The lab investigates bacterial flagella, including the basal body, hook, and filament, to understand their mechanical and dynamic properties at near-atomic resolution. A key research direction involves applying advanced cryoEM techniques to visualize the self-assembly and functional mechanisms of macromolecular machines in bacteria such as *Salmonella enterica* serovar Typhimurium. The lab also pioneers structural studies of DNA nanostructures, demonstrating the power of cryoEM for determining absolute stereochemistry and 3D architecture at unprecedented resolution.
Figures are computed from collected data and may differ slightly.
Many DNA nanostructures have been produced and a wide range of potential applications have been proposed. However, confirmation of accurate 3D construction is particularly challenging. Here, we demonstrate that cryoEM may be exploited to obtain structural information at sufficient resolution to visualize the DNA helix and reveal the absolute stereochemistry of a 7 nm self-assembled DNA tetrahedron. Structural analysis at such high resolution by cryoEM image analysis is unprecedented for any biol
The bacterial flagellum is a motility organelle consisting of a long helical filament as a propeller and a rotary motor that drives rapid filament rotation to produce thrust. <i>Salmonella</i><i>enterica</i> serovar Typhimurium has two genes of flagellin, <i>fljB</i> and <i>fliC</i>, for flagellar filament formation and autonomously switches their expression at a frequency of 10<sup>-3</sup>-10<sup>-4</sup> per cell per generation. We report here differences in their structures and motility func
Journal Article CryoTEM with a Cold Field Emission Gun That Moves Structural Biology into a New Stage Get access Takayuki Kato, Takayuki Kato Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan Search for other works by this author on: Oxford Academic Google Scholar Fumiaki Makino, Fumiaki Makino Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan Search for other works by this author on: Oxford Academic Google Scholar Takanori Nakane, Takano
The basal body of the bacterial flagellum is a rotary motor that consists of several rings (C, MS and LP) and a rod. The LP ring acts as a bushing supporting the distal rod for its rapid and stable rotation without much friction. Here, we use electron cryomicroscopy to describe the LP ring structure around the rod, at 3.5 Å resolution, from Salmonella Typhimurium. The structure shows 26-fold rotational symmetry and intricate intersubunit interactions of each subunit with up to six partners, whic
The Bacterial flagellar hook is a short supercoiled tubular structure made from a helical assembly of the hook protein FlgE. The hook acts as a universal joint that connects the flagellar basal body and filament, and smoothly transmits torque generated by the rotary motor to the helical filament propeller. In peritrichously flagellated bacteria, the hook allows the filaments to form a bundle behind the cell for swimming, and for the bundle to fall apart for tumbling. Here we report a native supe
The bacterial flagellum is a motility organelle consisting of a rotary motor and a long helical filament as a propeller. The flagellar hook is a flexible universal joint that transmits motor torque to the filament in its various orientations that change dynamically between swimming and tumbling of the cell upon switching the motor rotation for chemotaxis. Although the structures of the hook and hook protein FlgE from different bacterial species have been studied, the structure of <i>Salmonella</
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