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TitleCryo-EM structure of the bifunctional secretin complex of .
Journal, issue, pagesElife, Vol. 6, Year 2017
Publish dateDec 27, 2017
AuthorsEdoardo D'Imprima / Ralf Salzer / Ramachandra M Bhaskara / Ricardo Sánchez / Ilona Rose / Lennart Kirchner / Gerhard Hummer / Werner Kühlbrandt / Janet Vonck / Beate Averhoff /
PubMed AbstractSecretins form multimeric channels across the outer membrane of Gram-negative bacteria that mediate the import or export of substrates and/or extrusion of type IV pili. The secretin complex of is an ...Secretins form multimeric channels across the outer membrane of Gram-negative bacteria that mediate the import or export of substrates and/or extrusion of type IV pili. The secretin complex of is an oligomer of the 757-residue PilQ protein, essential for DNA uptake and pilus extrusion. Here, we present the cryo-EM structure of this bifunctional complex at a resolution of ~7 Å using a new reconstruction protocol. Thirteen protomers form a large periplasmic domain of six stacked rings and a secretin domain in the outer membrane. A homology model of the PilQ protein was fitted into the cryo-EM map. A crown-like structure outside the outer membrane capping the secretin was found not to be part of PilQ. Mutations in the secretin domain disrupted the crown and abolished DNA uptake, suggesting a central role of the crown in natural transformation.
External linksElife / PubMed:29280731 / PubMed Central
MethodsEM (single particle)
Resolution6.5 - 20.4 Å
Structure data

EMDB-3985:
PilQ from Thermus thermophilus
Method: EM (single particle) / Resolution: 20.4 Å

EMDB-3995:
Cap domain and N5 ring of PilQ from Thermus thermophilus
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-3996:
N4 ring of PilQ from Thermus thermophilus
Method: EM (single particle) / Resolution: 6.5 Å

EMDB-3997:
N2 and N3 ring of PilQ from Thermus thermophilus
Method: EM (single particle) / Resolution: 7.6 Å

EMDB-3998:
N0 and N1 ring of PilQ from Thermus thermophilus
Method: EM (single particle) / Resolution: 7.0 Å

Source
  • Thermus thermophilus HB27 (bacteria)

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