6GMS
Solution NMR structure of the major type IV pilin PpdD from enterohemorrhagic Escherichia coli (EHEC)
Summary for 6GMS
| Entry DOI | 10.2210/pdb6gms/pdb |
| NMR Information | BMRB: 18823 |
| Descriptor | Prepilin peptidase-dependent protein D (1 entity in total) |
| Functional Keywords | type iv pilin adhesion ehec t4p, cell adhesion |
| Biological source | Escherichia coli O157:H7 |
| Total number of polymer chains | 1 |
| Total formula weight | 14241.80 |
| Authors | Amorim, G.C.,Bardiaux, B.,Luna-Rico, A.,Zeng, W.,Guilvout, I.,Egelman, E.,Nilges, M.,Francetic, O.,Izadi-Pruneyre, N. (deposition date: 2018-05-28, release date: 2019-05-15, Last modification date: 2023-06-14) |
| Primary citation | Bardiaux, B.,de Amorim, G.C.,Luna Rico, A.,Zheng, W.,Guilvout, I.,Jollivet, C.,Nilges, M.,Egelman, E.H.,Izadi-Pruneyre, N.,Francetic, O. Structure and Assembly of the Enterohemorrhagic Escherichia coli Type 4 Pilus. Structure, 27:1082-1093.e5, 2019 Cited by PubMed Abstract: Bacterial type 4a pili are dynamic surface filaments that promote bacterial adherence, motility, and macromolecular transport. Their genes are highly conserved among enterobacteria and their expression in enterohemorrhagic Escherichia coli (EHEC) promotes adhesion to intestinal epithelia and pro-inflammatory signaling. To define the molecular basis of EHEC pilus assembly, we determined the structure of the periplasmic domain of its major subunit PpdD (PpdDp), a prototype of an enterobacterial pilin subfamily containing two disulfide bonds. The structure of PpdDp, determined by NMR, was then docked into the density envelope of purified EHEC pili obtained by cryoelectron microscopy (cryo-EM). Cryo-EM reconstruction of EHEC pili at ∼8 Å resolution revealed extremely high pilus flexibility correlating with a large extended region of the pilin stem. Systematic mutagenesis combined with functional and interaction analyses identified charged residues essential for pilus assembly. Structural information on exposed regions and interfaces between EHEC pilins is relevant for vaccine and drug discovery. PubMed: 31056419DOI: 10.1016/j.str.2019.03.021 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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