3GGH

Donor strand complemented FaeG of F4ad fimbriae

Summary for 3GGH

• Entry DOI: 10.2210/pdb3ggh/pdb
• Related: 2J6G 2J6R 3F65 3GEA 3GEW 3GFU 3HLR
• Descriptor: K88 fimbrial protein AD, SULFATE ION (3 entities in total)
• Functional Keywords: immunoglobulin like fold, fimbrium, cell adhesion
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 58528.84

Authors

Van Molle, I.,Moonens, K.,Garcia-Pino, A.,Buts, L.,Bouckaert, J.,De Greve, H. (deposition date: 2009-02-28, release date: 2009-10-20, Last modification date: 2023-11-01)

Primary citation

Van Molle, I.,Moonens, K.,Garcia-Pino, A.,Buts, L.,De Kerpel, M.,Wyns, L.,Bouckaert, J.,De Greve, H.
Structural and thermodynamic characterization of pre- and postpolymerization states in the F4 fimbrial subunit FaeG
J.Mol.Biol., 394:957-967, 2009

PubMed Abstract: Enterotoxigenic Escherichia coli expressing F4 fimbriae are the major cause of porcine colibacillosis and are responsible for significant death and morbidity in neonatal and postweaned piglets. Via the chaperone-usher pathway, F4 fimbriae are assembled into thin, flexible polymers mainly composed of the single-domain adhesin FaeG. The F4 fimbrial system has been labeled eccentric because the F4 pilins show some features distinct from the features of pilins of other chaperone-usher-assembled structures. In particular, FaeG is much larger than other pilins (27 versus approximately 17 kDa), grafting an additional carbohydrate binding domain on the common immunoglobulin-like core. Structural data of FaeG during different stages of the F4 fimbrial biogenesis process, combined with differential scanning calorimetry measurements, confirm the general principles of the donor strand complementation/exchange mechanisms taking place during pilus biogenesis via the chaperone-usher pathway.

PubMed: 19799915
DOI: 10.1016/j.jmb.2009.09.059

Experimental method

X-RAY DIFFRACTION (1.639 Å)