5LVY
Structural studies of the Aggregative Adherence Fimbriae of Enteroaggregative Escherichia coli
Summary for 5LVY
| Entry DOI | 10.2210/pdb5lvy/pdb |
| NMR Information | BMRB: 34042 |
| Descriptor | Adhesin protein (1 entity in total) |
| Functional Keywords | aggregative adherence fimbriae, donor strand complementation, eaec, e. coli, fibronectin, cell adhesion |
| Biological source | Escherichia coli O111:H21 |
| Total number of polymer chains | 1 |
| Total formula weight | 16493.50 |
| Authors | Liu, B.,Matthews, S. (deposition date: 2016-09-14, release date: 2017-07-26, Last modification date: 2024-10-23) |
| Primary citation | Jnsson, R.,Liu, B.,Struve, C.,Yang, Y.,Jrgensen, R.,Xu, Y.,Jenssen, H.,Krogfelt, K.A.,Matthews, S. Structural and functional studies of Escherichia coli aggregative adherence fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding. Biochim. Biophys. Acta, 1865:304-311, 2017 Cited by PubMed Abstract: Enteroaggregative Escherichia coli (EAEC) is an emerging cause of acute and persistent diarrhea worldwide. The pathogenesis of different EAEC stains is complicated, however, the early essential step begins with attachment of EAEC to intestinal mucosa via aggregative adherence fimbriae (AAFs). Currently, five different variants have been identified, which all share a degree of similarity in the gene organization of their operons and sequences. Here, we report the solution structure of Agg5A from the AAF/V variant. While preserving the major structural features shared by all AAF members, only Agg5A possesses an inserted helix at the beginning of the donor strand, which together with altered surface electrostatics, renders the protein unable to interact with fibronectin. Hence, here we characterize the first AAF variant with a binding mode that varies from previously described AAFs. PubMed: 27939608DOI: 10.1016/j.bbapap.2016.11.017 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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