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.
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Dates
Type | When |
---|---|
Created | 10 years, 3 months ago (May 21, 2015, 7:33 a.m.) |
Deposited | 1 year, 10 months ago (Oct. 11, 2023, 8:49 p.m.) |
Indexed | 3 weeks, 5 days ago (July 30, 2025, 1:07 p.m.) |
Issued | 10 years, 3 months ago (May 21, 2015) |
Published | 10 years, 3 months ago (May 21, 2015) |
Published Online | 10 years, 3 months ago (May 21, 2015) |
Funders
2
Max-Planck-Gesellschaft (Max Planck Society)
10.13039/501100004189
Max-Planck-GesellschaftRegion: Europe
gov (Research institutes and centers)
Labels
4
- Max Planck Society for the Advancement of Science
- Max-Planck-Gesellschaft zur Förderung der Wissenschaften
- Max Planck Society
- MPG
Deutsche Forschungsgemeinschaft (DFG)
10.13039/501100001659
Deutsche ForschungsgemeinschaftRegion: Europe
gov (National government)
Labels
3
- German Research Association
- German Research Foundation
- DFG
Awards
1
- AV 9/6-1
@article{Gold_2015, title={Structure of a type IV pilus machinery in the open and closed state}, volume={4}, ISSN={2050-084X}, url={http://dx.doi.org/10.7554/elife.07380}, DOI={10.7554/elife.07380}, journal={eLife}, publisher={eLife Sciences Publications, Ltd}, author={Gold, Vicki AM and Salzer, Ralf and Averhoff, Beate and Kühlbrandt, Werner}, year={2015}, month=may }