Structure of a type IV pilus machinery in the open and closed state

Gold, Vicky A. M.; Salzer, Ralf; Averhoff, Beate; Kühlbrandt, Werner

doi:10.7554/eLife.07380

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Structure of a type IV pilus machinery in the open and closed state

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Gold, Vicky A. M.
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Kühlbrandt, Werner
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Gold, V. A. M., Salzer, R., Averhoff, B., & Kühlbrandt, W. (2015). Structure of a type IV pilus machinery in the open and closed state. eLife, 4: e07380. doi:10.7554/eLife.07380.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0028-F017-6

Abstract

Proteins of the secretin family form large macromolecular complexes, which assemble in the outer membrane of Gram-negative bacteria. Secretins are major components of type II and III secretion systems and are linked to extrusion of type IV pili (T4P) and to DNA uptake. By electron cryo-tomography of whole Thermus thermophilus cells, we determined the in situ structure of a T4P molecular machine in the open and the closed state. Comparison reveals a major conformational change whereby the N-terminal domains of the central secretin PilQ shift by ∼30 Å, and two periplasmic gates open to make way for pilus extrusion. Furthermore, we determine the structure of the assembled pilus.