TY  - JOUR
AU  - Van Molle, I.
AU  - Moonens, K.
AU  - Buts, L.
AU  - Garcia-Pino, A.
AU  - Panjikar, S.
AU  - Wyns, L.
AU  - De Greve, H.
AU  - Bouckaert, J.
AU  - DESY
TI  - The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
JO  - Acta crystallographica / D
VL  - 65
SN  - 0907-4449
CY  - Copenhagen
PB  - Munksgaard
M1  - PHPPUBDB-12662
SP  - 411-420
PY  - 2009
N1  - © International Union of Crystallography; Post referee fulltext in progress 
AB  - 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.
KW  - Adhesins, Escherichia coli: chemistry
KW  - Calorimetry, Differential Scanning
KW  - Cross-Linking Reagents: pharmacology
KW  - Crystallography, X-Ray
KW  - Dimerization
KW  - Escherichia coli: chemistry
KW  - Escherichia coli: genetics
KW  - Escherichia coli Proteins: chemistry
KW  - Escherichia coli Proteins: genetics
KW  - Escherichia coli Proteins: isolation & purification
KW  - Escherichia coli Proteins: metabolism
KW  - Fimbriae Proteins: metabolism
KW  - Glutaral: pharmacology
KW  - Models, Molecular
KW  - Molecular Chaperones: chemistry
KW  - Molecular Chaperones: genetics
KW  - Molecular Chaperones: isolation & purification
KW  - Molecular Chaperones: metabolism
KW  - Nephelometry and Turbidimetry
KW  - Protein Conformation
KW  - Protein Denaturation
KW  - Protein Interaction Mapping
KW  - Recombinant Fusion Proteins: chemistry
KW  - Recombinant Fusion Proteins: isolation & purification
KW  - Adhesins, Escherichia coli (NLM Chemicals)
KW  - Cross-Linking Reagents (NLM Chemicals)
KW  - Escherichia coli Proteins (NLM Chemicals)
KW  - FaeG protein, E coli (NLM Chemicals)
KW  - Molecular Chaperones (NLM Chemicals)
KW  - Recombinant Fusion Proteins (NLM Chemicals)
KW  - Glutaral (NLM Chemicals)
KW  - faeE protein, E coli (NLM Chemicals)
KW  - Fimbriae Proteins (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:19390146
UR  - <Go to ISI:>//WOS:000265267000002
DO  - DOI:10.1107/S0907444909005174
UR  - https://bib-pubdb1.desy.de/record/94240
ER  -