4B4R

Crystal Structure of the lectin domain of F18 fimbrial adhesin FedF in complex with blood group B type 1 hexasaccharide

4B4R の概要

• エントリーDOI: 10.2210/pdb4b4r/pdb
• 関連するPDBエントリー: 4B4P 4B4Q
• 分子名称: F18 FIMBRIAL ADHESIN AC, alpha-L-fucopyranose-(1-2)-[alpha-D-galactopyranose-(1-3)]beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-alpha-D-glucopyranose (3 entities in total)
• 機能のキーワード: cell adhesion, fimbriae, bacterial adhesins, protein-carbohydrate interactions, abh blood group binding
• 由来する生物種: ESCHERICHIA COLI K-12
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34654.15

構造登録者

Moonens, K.,Bouckaert, J.,Coddens, A.,Tran, T.,Panjikar, S.,De Kerpel, M.,Cox, E.,Remaut, H.,De Greve, H. (登録日: 2012-07-31, 公開日: 2012-08-15, 最終更新日: 2024-10-23)

主引用文献

Moonens, K.,Bouckaert, J.,Coddens, A.,Tran, T.,Panjikar, S.,De Kerpel, M.,Cox, E.,Remaut, H.,De Greve, H.
Structural Insight in Histo-Blood Group Binding by the F18 Fimbrial Adhesin Fedf.
Mol.Microbiol., 86:82-, 2012

PubMed Abstract: F18-positive enterotoxigenic and Shiga toxin-producing Escherichia coli are responsible for post-weaning diarrhoea and oedema disease in pigs and lead to severe production losses in the farming industry. F18 fimbriae attach to the small intestine of young piglets by latching onto glycosphingolipids with A/H blood group determinants on type 1 core. We demonstrate the N-terminal domain of the F18 fimbrial subunit FedF to be responsible for ABH-mediated attachment and present its X-ray structure in ligand-free form and bound to A and B type 1 hexaoses. The FedF lectin domain comprises a 10-stranded immunoglobulin-like β-sandwich. Three linear motives, Q(47) -N(50), H(88) -S(90) and R(117) -T(119), form a shallow glycan binding pocket near the tip of the domain that is selective for type 1 core glycans in extended conformation. In addition to the glycan binding pocket, a polybasic loop on the membrane proximal surface of FedF lectin domain is shown to be required for binding to piglet enterocytes. Although dispensable for ABH glycan recognition, the polybasic surface adds binding affinity in the context of the host cell membrane, a mechanism that is proposed to direct ABH-glycan binding to cell-bound glycosphingolipids and could allow bacteria to avoid clearance by secreted glycoproteins.

PubMed: 22812428
DOI: 10.1111/J.1365-2958.2012.08174.X

実験手法

X-RAY DIFFRACTION (1.8 Å)