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The F4 fimbrial chaperone FaeE does not self-cap its interactive surfaces

X-ray diffraction
2.29Å resolution
PDB entry 3f65 coloured by chain, front view.
PDB entry 3f65 coloured by chain, side view.
PDB entry 3f65 coloured by chain, top view.
Source organism: Escherichia coli
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 11158.75 Å2
Buried surface area: 430.94 Å2
Dissociation area: 72.48 Å2
Dissociation energy (ΔGdiss): 3.8 kcal/mol
Dissociation entropy (TΔSdiss): 0.63 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459
Assembly 2
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 11077.49 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459
Assembly 3
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 10963.18 Å2
Buried surface area: 378.9 Å2
Dissociation area: 189.45 Å2
Dissociation energy (ΔGdiss): 13.71 kcal/mol
Dissociation entropy (TΔSdiss): 1.41 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459
Assembly 4
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 9279.51 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459
Assembly 5
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 10720.14 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459
Assembly 6
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 9557.14 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459
Assembly 7
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 10614.38 Å2
Buried surface area: 388.36 Å2
Dissociation area: 194.18 Å2
Dissociation energy (ΔGdiss): 12.08 kcal/mol
Dissociation entropy (TΔSdiss): 1.44 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459
Assembly 8
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Assembly Name: Chaperone protein FaeE
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Multimeric state: monomeric
Accessible surface area: 8547.21 Å2
Buried surface area: 0.0 Å2
Dissociation area: 0 Å2
Dissociation energy (ΔGdiss): 0 kcal/mol
Dissociation entropy (TΔSdiss): 0 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-150459

Macromolecules

Chaperone protein FaeE
Chains: A, B, C, D, E, F, G, H
Length: 224 amino acids
Theoretical weight: 24.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P25401 (Residues: 35-258; Coverage: 100%)
Gene name: faeE
Pfam: Pili and flagellar-assembly chaperone, PapD N-terminal domain
InterPro:
CATH: Immunoglobulins
Chaperone protein FaeE in PDB entry 3f65, assembly 1, front view.
Chaperone protein FaeE in PDB entry 3f65, assembly 1, side view.
Chaperone protein FaeE in PDB entry 3f65, assembly 1, top view.
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