4B4Q

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

Summary for 4B4Q

• Entry DOI: 10.2210/pdb4b4q/pdb
• Related: 4B4P 4B4R
• Descriptor: F18 FIMBRIAL ADHESIN AC, alpha-L-fucopyranose-(1-2)-[2-acetamido-2-deoxy-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)
• Functional Keywords: cell adhesion, bacterial adhesins, protein-carbohydrate interactions, abh blood group binding, stec, etec, spr, mst, bsi
• Biological source: ESCHERICHIA COLI K-12
• Total number of polymer chains: 2
• Total formula weight: 34736.25

Authors

Moonens, K.,Bouckaert, J.,Coddens, A.,Tran, T.,Panjikar, S.,De Kerpel, M.,Cox, E.,Remaut, H.,De Greve, H. (deposition date: 2012-07-31, release date: 2012-08-15, Last modification date: 2024-11-06)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2 Å)