7ZL4
Cryo-EM structure of archaic chaperone-usher Csu pilus of Acinetobacter baumannii
Summary for 7ZL4
| Entry DOI | 10.2210/pdb7zl4/pdb |
| Related | 6FM5 |
| EMDB information | 14777 |
| Descriptor | CsuA/B (1 entity in total) |
| Functional Keywords | chaperone-usher pathway, bacterial adhesion, biofilm formation, acinetobacter baumannii, csu pili, cell adhesion |
| Biological source | Acinetobacter baumannii |
| Total number of polymer chains | 4 |
| Total formula weight | 64278.57 |
| Authors | Pakharukova, N.,Malmi, H.,Tuittila, M.,Paavilainen, S.,Ghosal, D.,Chang, Y.W.,Jensen, G.J.,Zavialov, A.V. (deposition date: 2022-04-13, release date: 2022-08-03, Last modification date: 2024-10-23) |
| Primary citation | Pakharukova, N.,Malmi, H.,Tuittila, M.,Dahlberg, T.,Ghosal, D.,Chang, Y.W.,Myint, S.L.,Paavilainen, S.,Knight, S.D.,Lamminmaki, U.,Uhlin, B.E.,Andersson, M.,Jensen, G.,Zavialov, A.V. Archaic chaperone-usher pili self-secrete into superelastic zigzag springs. Nature, 609:335-340, 2022 Cited by PubMed Abstract: Adhesive pili assembled through the chaperone-usher pathway are hair-like appendages that mediate host tissue colonization and biofilm formation of Gram-negative bacteria. Archaic chaperone-usher pathway pili, the most diverse and widespread chaperone-usher pathway adhesins, are promising vaccine and drug targets owing to their prevalence in the most troublesome multidrug-resistant pathogens. However, their architecture and assembly-secretion process remain unknown. Here, we present the cryo-electron microscopy structure of the prototypical archaic Csu pilus that mediates biofilm formation of Acinetobacter baumannii-a notorious multidrug-resistant nosocomial pathogen. In contrast to the thick helical tubes of the classical type 1 and P pili, archaic pili assemble into an ultrathin zigzag architecture secured by an elegant clinch mechanism. The molecular clinch provides the pilus with high mechanical stability as well as superelasticity, a property observed for the first time, to our knowledge, in biomolecules, while enabling a more economical and faster pilus production. Furthermore, we demonstrate that clinch formation at the cell surface drives pilus secretion through the outer membrane. These findings suggest that clinch-formation inhibitors might represent a new strategy to fight multidrug-resistant bacterial infections. PubMed: 35853476DOI: 10.1038/s41586-022-05095-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.45 Å) |
Structure validation
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