3JWN

Complex of FimC, FimF, FimG and FimH


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.69 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.245 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting.

Le Trong, I.Aprikian, P.Kidd, B.A.Forero-Shelton, M.Tchesnokova, V.Rajagopal, P.Rodriguez, V.Interlandi, G.Klevit, R.Vogel, V.Stenkamp, R.E.Sokurenko, E.V.Thomas, W.E.

(2010) Cell 141: 645-655

  • DOI: https://doi.org/10.1016/j.cell.2010.03.038
  • Primary Citation of Related Structures:  
    3JWN

  • PubMed Abstract: 

    The Escherichia coli fimbrial adhesive protein, FimH, mediates shear-dependent binding to mannosylated surfaces via force-enhanced allosteric catch bonds, but the underlying structural mechanism was previously unknown. Here we present the crystal structure of FimH incorporated into the multiprotein fimbrial tip, where the anchoring (pilin) domain of FimH interacts with the mannose-binding (lectin) domain and causes a twist in the beta sandwich fold of the latter. This loosens the mannose-binding pocket on the opposite end of the lectin domain, resulting in an inactive low-affinity state of the adhesin. The autoinhibition effect of the pilin domain is removed by application of tensile force across the bond, which separates the domains and causes the lectin domain to untwist and clamp tightly around the ligand like a finger-trap toy. Thus, beta sandwich domains, which are common in multidomain proteins exposed to tensile force in vivo, can undergo drastic allosteric changes and be subjected to mechanical regulation.


  • Organizational Affiliation

    Department of Biological Structure, Box 357420, University of Washington, Seattle, WA 98195, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Chaperone protein fimCA [auth C],
F [auth I]
205Escherichia coli K-12Mutation(s): 0 
Gene Names: b4316fimCJW4279
UniProt
Find proteins for P31697 (Escherichia coli (strain K12))
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Go to UniProtKB:  P31697
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UniProt GroupP31697
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Protein fimFB [auth E],
C [auth F],
G [auth K],
H [auth L]
154Escherichia coli K-12Mutation(s): 0 
Gene Names: b4318fimFJW4281
UniProt
Find proteins for P08189 (Escherichia coli (strain K12))
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Go to UniProtKB:  P08189
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UniProt GroupP08189
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  • Reference Sequence
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Protein fimGD [auth G],
I [auth M]
144Escherichia coli K-12Mutation(s): 0 
Gene Names: b4319fimGJW4282
UniProt
Find proteins for P08190 (Escherichia coli (strain K12))
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UniProt GroupP08190
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  • Reference Sequence
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
FimH proteinE [auth H],
J [auth N]
279Escherichia coli F18+Mutation(s): 0 
Gene Names: ECP_4655fimh
UniProt
Find proteins for A0A0R4I961 (Escherichia coli F18+)
Explore A0A0R4I961 
Go to UniProtKB:  A0A0R4I961
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UniProt GroupA0A0R4I961
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.69 Å
  • R-Value Free: 0.272 
  • R-Value Work: 0.244 
  • R-Value Observed: 0.245 
  • Space Group: H 3 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 216.025α = 90
b = 216.025β = 90
c = 532.072γ = 120
Software Package:
Software NamePurpose
PHASERphasing
MOLREPphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2010-06-16
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2023-09-06
    Changes: Data collection, Database references, Derived calculations, Refinement description