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TitleStructure of a type IV pilus machinery in the open and closed state.
Journal, issue, pagesElife, Vol. 4, Year 2015
Publish dateMay 21, 2015
AuthorsVicki A M Gold / Ralf Salzer / Beate Averhoff / Werner Kühlbrandt /
PubMed AbstractProteins 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.
External linksElife / PubMed:25997099 / PubMed Central
MethodsEM (subtomogram averaging)
Resolution32.0 - 45.0 Å
Structure data

EMDB-3021:
Structure of the type IV pilus machinery from Thermus thermophilus in the closed state
Method: EM (subtomogram averaging) / Resolution: 40.0 Å

EMDB-3022:
Structure of the type IV pilus machinery from Thermus thermophilus in the closed state
Method: EM (subtomogram averaging) / Resolution: 35.0 Å

EMDB-3023:
Structure of the type IV pilus machinery from Thermus thermophilus in the open state
Method: EM (subtomogram averaging) / Resolution: 45.0 Å

EMDB-3024:
Structure of the type IV pilus from Thermus thermophilus
Method: EM (subtomogram averaging) / Resolution: 32.0 Å

Source
  • Thermus thermophilus HB27 (bacteria)

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