3F6I

Structure of the SeMet labeled F4 fibrial chaperone FaeE

Summary for 3F6I

• Entry DOI: 10.2210/pdb3f6i/pdb
• Related: 3F65 3F6L
• Descriptor: Chaperone protein faeE (2 entities in total)
• Functional Keywords: immunoglobulin-like fold, cell projection, chaperone, fimbrium, immunoglobulin domain, periplasm, plasmid
• Biological source: Escherichia coli
• Cellular location: Periplasm: P25401
• Total number of polymer chains: 2
• Total formula weight: 49977.60

Authors

Van Molle, I.,Moonens, K.,Buts, L.,Garcia-Pino, A.,Wyns, L.,De Greve, H.,Bouckaert, J. (deposition date: 2008-11-06, release date: 2009-05-19, Last modification date: 2023-12-27)

Primary citation

Van Molle, I.,Moonens, K.,Buts, L.,Garcia-Pino, A.,Panjikar, S.,Wyns, L.,De Greve, H.,Bouckaert, J.
The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
Acta Crystallogr.,Sect.D, 65:411-420, 2009

PubMed 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.

PubMed: 19390146
DOI: 10.1107/S0907444909005174

Experimental method

X-RAY DIFFRACTION (2.788 Å)