6E14

Handover mechanism of the growing pilus by the bacterial outer membrane usher FimD


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD.

Du, M.Yuan, Z.Yu, H.Henderson, N.Sarowar, S.Zhao, G.Werneburg, G.T.Thanassi, D.G.Li, H.

(2018) Nature 562: 444-447

  • DOI: https://doi.org/10.1038/s41586-018-0587-z
  • Primary Citation of Related Structures:  
    6E14, 6E15

  • PubMed Abstract: 

    Pathogenic bacteria such as Escherichia coli assemble surface structures termed pili, or fimbriae, to mediate binding to host-cell receptors 1 . Type 1 pili are assembled via the conserved chaperone-usher pathway 2-5 . The outer-membrane usher FimD recruits pilus subunits bound by the chaperone FimC via the periplasmic N-terminal domain of the usher. Subunit translocation through the β-barrel channel of the usher occurs at the two C-terminal domains (which we label CTD1 and CTD2) of this protein. How the chaperone-subunit complex bound to the N-terminal domain is handed over to the C-terminal domains, as well as the timing of subunit polymerization into the growing pilus, have previously been unclear. Here we use cryo-electron microscopy to capture a pilus assembly intermediate (FimD-FimC-FimF-FimG-FimH) in a conformation in which FimD is in the process of handing over the chaperone-bound end of the growing pilus to the C-terminal domains. In this structure, FimF has already polymerized with FimG, and the N-terminal domain of FimD swings over to bind CTD2; the N-terminal domain maintains contact with FimC-FimF, while at the same time permitting access to the C-terminal domains. FimD has an intrinsically disordered N-terminal tail that precedes the N-terminal domain. This N-terminal tail folds into a helical motif upon recruiting the FimC-subunit complex, but reorganizes into a loop to bind CTD2 during handover. Because both the N-terminal and C-terminal domains of FimD are bound to the end of the growing pilus, the structure further suggests a mechanism for stabilizing the assembly intermediate to prevent the pilus fibre diffusing away during the incorporation of thousands of subunits.


  • Organizational Affiliation

    Structural Biology Program, Van Andel Research Institute, Grand Rapids, MI, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Type 1 fimbrin D-mannose specific adhesinA [auth H]300Escherichia coliMutation(s): 0 
Gene Names: fimHb4320JW4283
Membrane Entity: Yes 
UniProt
Find proteins for P08191 (Escherichia coli (strain K12))
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Go to UniProtKB:  P08191
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UniProt GroupP08191
Sequence Annotations
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Fimbrial biogenesis outer membrane usher proteinB [auth D]879Escherichia coliMutation(s): 0 
Gene Names: fimD_3APZ14_00735AW106_26365COD30_02575CXB56_24500ERS085374_04437ERS150876_04614FORC28_5312
Membrane Entity: Yes 
UniProt
Find proteins for P30130 (Escherichia coli (strain K12))
Explore P30130 
Go to UniProtKB:  P30130
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UniProt GroupP30130
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Protein FimFC [auth F]156Escherichia coliMutation(s): 0 
Gene Names: fimFb4318JW4281
Membrane Entity: Yes 
UniProt
Find proteins for P08189 (Escherichia coli (strain K12))
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UniProt GroupP08189
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Protein FimGD [auth G]158Escherichia coliMutation(s): 0 
Gene Names: fimGb4319JW4282
Membrane Entity: Yes 
UniProt
Find proteins for P08190 (Escherichia coli (strain K12))
Explore P08190 
Go to UniProtKB:  P08190
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UniProt GroupP08190
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Chaperone protein FimCE [auth C]241Escherichia coliMutation(s): 0 
Gene Names: fimCb4316JW4279
Membrane Entity: Yes 
UniProt
Find proteins for P31697 (Escherichia coli (strain K12))
Explore P31697 
Go to UniProtKB:  P31697
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UniProt GroupP31697
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.00 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

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Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)United StatesGM062987

Revision History  (Full details and data files)

  • Version 1.0: 2018-10-17
    Type: Initial release
  • Version 1.1: 2018-10-31
    Changes: Data collection, Database references
  • Version 1.2: 2019-12-18
    Changes: Author supporting evidence