4WEM
Co-complex structure of the F4 fimbrial adhesin FaeG variant ac with llama single domain antibody V1
Summary for 4WEM
| Entry DOI | 10.2210/pdb4wem/pdb |
| Related | 3HLR |
| Descriptor | K88 fimbrial protein AC, Anti-F4+ETEC bacteria VHH variable region, PHOSPHATE ION, ... (4 entities in total) |
| Functional Keywords | complex, llama single domain antibody, adhesin, nanobody, structural protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 2 |
| Total formula weight | 43062.34 |
| Authors | Moonens, K.,Van den Broeck, I.,Pardon, E.,De Kerpel, M.,Remaut, H.,De Greve, H. (deposition date: 2014-09-10, release date: 2015-02-04, Last modification date: 2024-10-16) |
| Primary citation | Moonens, K.,Van den Broeck, I.,Okello, E.,Pardon, E.,De Kerpel, M.,Remaut, H.,De Greve, H. Structural insight in the inhibition of adherence of F4 fimbriae producing enterotoxigenic Escherichia coli by llama single domain antibodies. Vet. Res., 46:14-14, 2015 Cited by PubMed Abstract: Enterotoxigenic Escherichia coli that cause neonatal and post-weaning diarrhea in piglets express F4 fimbriae to mediate attachment towards host receptors. Recently we described how llama single domain antibodies (VHHs) fused to IgA, produced in Arabidopsis thaliana seeds and fed to piglets resulted in a progressive decline in shedding of F4 positive ETEC bacteria. Here we present the structures of these inhibiting VHHs in complex with the major adhesive subunit FaeG. A conserved surface, distant from the lactose binding pocket, is targeted by these VHHs, highlighting the possibility of targeting epitopes on single-domain adhesins that are non-involved in receptor binding. PubMed: 25828907DOI: 10.1186/s13567-015-0151-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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