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-Structure paper
Title | Structure of a type IV pilus machinery in the open and closed state. |
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Journal, issue, pages | Elife, Vol. 4, Year 2015 |
Publish date | May 21, 2015 |
![]() | Vicki A M Gold / Ralf Salzer / Beate Averhoff / Werner Kühlbrandt / ![]() |
PubMed 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 ...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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Methods | EM (subtomogram averaging) |
Resolution | 32.0 - 45.0 Å |
Structure data | ![]() EMDB-3021: ![]() EMDB-3022: ![]() EMDB-3023: ![]() EMDB-3024: |
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