5JXL

Cryo-EM structure of the flagellar hook of Campylobacter jejuni

Summary for 5JXL

• Entry DOI: 10.2210/pdb5jxl/pdb
• EMDB information: 8179
• Descriptor: flagellar hook protein FlgE (1 entity in total)
• Functional Keywords: campylobacter jejuni, helical assembly of flge, flagellar hook, motor protein
• Biological source: Campylobacter jejuni subsp. jejuni 81116
• Total number of polymer chains: 1
• Total formula weight: 90449.75

Authors

Matsunami, H.,Wolf, M.,Samatey, F.A. (deposition date: 2016-05-13, release date: 2016-11-16, Last modification date: 2024-03-20)

Primary citation

Matsunami, H.,Barker, C.S.,Yoon, Y.H.,Wolf, M.,Samatey, F.A.
Complete structure of the bacterial flagellar hook reveals extensive set of stabilizing interactions
Nat Commun, 7:13425-13425, 2016

PubMed Abstract: The bacterial flagellar hook is a tubular helical structure made by the polymerization of multiple copies of a protein, FlgE. Here we report the structure of the hook from Campylobacter jejuni by cryo-electron microscopy at a resolution of 3.5 Å. On the basis of this structure, we show that the hook is stabilized by intricate inter-molecular interactions between FlgE molecules. Extra domains in FlgE, found only in Campylobacter and in related bacteria, bring more stability and robustness to the hook. Functional experiments suggest that Campylobacter requires an unusually strong hook to swim without its flagella being torn off. This structure reveals details of the quaternary organization of the hook that consists of 11 protofilaments. Previous study of the flagellar filament of Campylobacter by electron microscopy showed its quaternary structure made of seven protofilaments. Therefore, this study puts in evidence the difference between the quaternary structures of a bacterial filament and its hook.

PubMed: 27811912
DOI: 10.1038/ncomms13425

Experimental method

ELECTRON MICROSCOPY (3.5 Å)