2J6R

FaeG from F4ac ETEC strain GIS26, produced in tobacco plant chloroplast

2J6R の概要

• エントリーDOI: 10.2210/pdb2j6r/pdb
• 関連するPDBエントリー: 2J6G
• 分子名称: K88 FIMBRIAL PROTEIN, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: plasmid, fimbria, ig-fold, f4 fimbriae, chaperone-usher pathway, cell adhesion, strand swapping, chloroplast targeting
• 由来する生物種: ESCHERICHIA COLI; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 56366.02

構造登録者

Van Molle, I.,Joensuu, J.J.,Buts, L.,Panjikar, S.,Kotiaho, M.,Bouckaert, J.,Wyns, L.,Niklander-Teeri, V.,De Greve, H. (登録日: 2006-10-03, 公開日: 2007-04-10, 最終更新日: 2023-12-13)

主引用文献

Van Molle, I.,Joensuu, J.J.,Buts, L.,Panjikar, S.,Kotiaho, M.,Bouckaert, J.,Wyns, L.,Niklander-Teeri, V.,De Greve, H.
Chloroplasts Assemble the Major Subunit Faeg of Escherichia Coli F4 (K88) Fimbriae Into Strand-Swapped Dimers
J.Mol.Biol., 368:791-, 2007

PubMed Abstract: F4 fimbriae encoded by the fae operon are the major colonization factors associated with porcine neonatal and postweaning diarrhoea caused by enterotoxigenic Escherichia coli (ETEC). Via the chaperone/usher pathway, the F4 fimbriae are assembled as long polymers of the major subunit FaeG, which also possesses the adhesive properties of the fimbriae. Intrinsically, the incomplete fold of fimbrial subunits renders them unstable and susceptible to aggregation and/or proteolytic degradation in the absence of a specific periplasmic chaperone. In order to test the possibility of producing FaeG in plants, FaeG expression was studied in transgenic tobacco plants. FaeG was directed to different subcellular compartments by specific targeting signals. Targeting of FaeG to the chloroplast results in much higher yields than FaeG targeting to the endoplasmic reticulum or the apoplast. Two chloroplast-targeted FaeG variants were purified from tobacco plants and crystallized. The crystal structures show that chloroplasts circumvent the absence of the fimbrial assembly machinery by assembling FaeG into strand-swapped dimers. Furthermore, the structures reveal how FaeG combines the structural requirements of a major fimbrial subunit with its adhesive role by grafting an additional domain on its Ig-like core.

PubMed: 17368480
DOI: 10.1016/J.JMB.2007.02.051

実験手法

X-RAY DIFFRACTION (1.9 Å)