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@ARTICLE{VanMolle:94240,
      author       = {Van Molle, I. and Moonens, K. and Buts, L. and Garcia-Pino,
                      A. and Panjikar, S. and Wyns, L. and De Greve, H. and
                      Bouckaert, J. and DESY},
      title        = {{T}he {F}4 fimbrial chaperone {F}ae{E} is stable as a
                      monomer that does not require self-capping of its
                      pilin-interactive surfaces},
      journal      = {Acta crystallographica / D},
      volume       = {65},
      issn         = {0907-4449},
      address      = {Copenhagen},
      publisher    = {Munksgaard},
      reportid     = {PHPPUBDB-12662},
      pages        = {411-420},
      year         = {2009},
      note         = {© International Union of Crystallography; Post referee
                      fulltext in progress},
      abstract     = {Many Gram-negative bacteria use the chaperone-usher pathway
                      to express adhesive surface structures, such as fimbriae, in
                      order to mediate attachment to host cells. Periplasmic
                      chaperones are required to shuttle fimbrial subunits or
                      pilins through the periplasmic space in an
                      assembly-competent form. The chaperones cap the hydrophobic
                      surface of the pilins through a donor-strand complementation
                      mechanism. FaeE is the periplasmic chaperone required for
                      the assembly of the F4 fimbriae of enterotoxigenic
                      Escherichia coli. The FaeE crystal structure shows a dimer
                      formed by interaction between the pilin-binding interfaces
                      of the two monomers. Dimerization and tetramerization have
                      been observed previously in crystal structures of fimbrial
                      chaperones and have been suggested to serve as a
                      self-capping mechanism that protects the pilin-interactive
                      surfaces in solution in the absence of the pilins. However,
                      thermodynamic and biochemical data show that FaeE occurs as
                      a stable monomer in solution. Other lines of evidence
                      indicate that self-capping of the pilin-interactive
                      interfaces is not a mechanism that is conservedly applied by
                      all periplasmic chaperones, but is rather a case-specific
                      solution to cap aggregation-prone surfaces.},
      keywords     = {Adhesins, Escherichia coli: chemistry / Calorimetry,
                      Differential Scanning / Cross-Linking Reagents: pharmacology
                      / Crystallography, X-Ray / Dimerization / Escherichia coli:
                      chemistry / Escherichia coli: genetics / Escherichia coli
                      Proteins: chemistry / Escherichia coli Proteins: genetics /
                      Escherichia coli Proteins: isolation $\&$ purification /
                      Escherichia coli Proteins: metabolism / Fimbriae Proteins:
                      metabolism / Glutaral: pharmacology / Models, Molecular /
                      Molecular Chaperones: chemistry / Molecular Chaperones:
                      genetics / Molecular Chaperones: isolation $\&$ purification
                      / Molecular Chaperones: metabolism / Nephelometry and
                      Turbidimetry / Protein Conformation / Protein Denaturation /
                      Protein Interaction Mapping / Recombinant Fusion Proteins:
                      chemistry / Recombinant Fusion Proteins: isolation $\&$
                      purification / Adhesins, Escherichia coli (NLM Chemicals) /
                      Cross-Linking Reagents (NLM Chemicals) / Escherichia coli
                      Proteins (NLM Chemicals) / FaeG protein, E coli (NLM
                      Chemicals) / Molecular Chaperones (NLM Chemicals) /
                      Recombinant Fusion Proteins (NLM Chemicals) / Glutaral (NLM
                      Chemicals) / faeE protein, E coli (NLM Chemicals) / Fimbriae
                      Proteins (NLM Chemicals)},
      cin          = {EMBL(-2012)},
      ddc          = {570},
      cid          = {$I:(DE-H253)EMBL_-2012_-20130307$},
      pnm          = {FS Beamline without reference (POF1-550)},
      pid          = {G:(DE-H253)POF1-No-Ref-20130405},
      experiment   = {EXP:(DE-H253)Unknown-BL-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:19390146},
      UT           = {WOS:000265267000002},
      doi          = {10.1107/S0907444909005174},
      url          = {https://bib-pubdb1.desy.de/record/94240},
}