6JZR

Structure of the bacterial flagellar polyrod

Summary for 6JZR

• Entry DOI: 10.2210/pdb6jzr/pdb
• EMDB information: 6683
• Descriptor: Flagellar basal-body rod protein FlgG (1 entity in total)
• Functional Keywords: bacterial flagellum, rod protein, structural protein, motor protein
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 22
• Total formula weight: 612191.51

Authors

Saijo-Hamano, Y.,Matsunami, H.,Namba, K.,Imada, K. (deposition date: 2019-05-03, release date: 2019-07-17, Last modification date: 2025-07-02)

Primary citation

Saijo-Hamano, Y.,Matsunami, H.,Namba, K.,Imada, K.
Architecture of the Bacterial Flagellar Distal Rod and Hook ofSalmonella.
Biomolecules, 9:-, 2019

PubMed Abstract: The bacterial flagellum is a large molecular complex composed of thousands of protein subunits for motility. The filamentous part of the flagellum, which is called the axial structure, consists of the filament, the hook, and the rods, with other minor components-the cap protein and the hook associated proteins. They share a common basic architecture of subunit arrangement, but each part shows quite distinct mechanical properties to achieve its specific function. The distal rod and the hook are helical assemblies of a single protein, FlgG and FlgE, respectively. They show a significant sequence similarity but have distinct mechanical characteristics. The rod is a rigid, straight cylinder, whereas the hook is a curved tube with high bending flexibility. Here, we report a structural model of the rod constructed by using the crystal structure of a core fragment of FlgG with a density map obtained previously by electron cryomicroscopy. Our structural model suggests that a segment called L-stretch plays a key role in achieving the distinct mechanical properties of the rod using a structurally similar component protein to that of the hook.

PubMed: 31284631
DOI: 10.3390/biom9070260

Experimental method

ELECTRON MICROSCOPY (7.4 Å)