1WLG

Crystal structure of FlgE31, a major fragment of the hook protein

Summary for 1WLG

• Entry DOI: 10.2210/pdb1wlg/pdb
• Related: 1IO1 1UCU
• Descriptor: Flagellar hook protein flgE (2 entities in total)
• Functional Keywords: ear-& motif, structural protein
• Biological source: Salmonella typhimurium
• Cellular location: Bacterial flagellum basal body (By similarity): P0A1J1
• Total number of polymer chains: 2
• Total formula weight: 62670.17

Authors

Samatey, F.A.,Matsunami, H.,Imada, K.,Nagashima, S.,Shaikh, T.R.,Thomas, D.R.,DeRosier, D.J.,Kitao, A.,Namba, K. (deposition date: 2004-06-25, release date: 2004-11-02, Last modification date: 2024-03-13)

Primary citation

Samatey, F.A.,Matsunami, H.,Imada, K.,Nagashima, S.,Shaikh, T.R.,Thomas, D.R.,Chen, J.Z.,Derosier, D.J.,Kitao, A.,Namba, K.
Structure of the bacterial flagellar hook and implication for the molecular universal joint mechanism.
Nature, 431:1062-1068, 2004

PubMed Abstract: The bacterial flagellum is a motile organelle, and the flagellar hook is a short, highly curved tubular structure that connects the flagellar motor to the long filament acting as a helical propeller. The hook is made of about 120 copies of a single protein, FlgE, and its function as a nano-sized universal joint is essential for dynamic and efficient bacterial motility and taxis. It transmits the motor torque to the helical propeller over a wide range of its orientation for swimming and tumbling. Here we report a partial atomic model of the hook obtained by X-ray crystallography of FlgE31, a major proteolytic fragment of FlgE lacking unfolded terminal regions, and by electron cryomicroscopy and three-dimensional helical image reconstruction of the hook. The model reveals the intricate molecular interactions and a plausible switching mechanism for the hook to be flexible in bending but rigid against twisting for its universal joint function.

PubMed: 15510139
DOI: 10.1038/nature02997

Experimental method

X-RAY DIFFRACTION (1.8 Å)