3HLR

Donor strand complemented FaeG of F4ad fimbriae

3HLR の概要

• エントリーDOI: 10.2210/pdb3hlr/pdb
• 関連するPDBエントリー: 2J6G 2J6R 3GEA 3GEW 3GFU 3GGH
• 分子名称: K88 fimbrial protein AD (2 entities in total)
• 機能のキーワード: immunoglobuline like fold, fimbrium, cell adhesion
• 由来する生物種: Escherichia coli; 詳細
• 細胞内の位置: Fimbrium: P14191
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28344.38

構造登録者

Van Molle, I.,Moonens, K.,Garcia-Pino, A.,Buts, L.,Bouckaert, J.,De Greve, H. (登録日: 2009-05-28, 公開日: 2009-10-20, 最終更新日: 2024-03-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.3 Å)