7ZN2
Tail tip of siphophage T5 : full complex after interaction with its bacterial receptor FhuA
This is a non-PDB format compatible entry.
Summary for 7ZN2
| Entry DOI | 10.2210/pdb7zn2/pdb |
| EMDB information | 14799 |
| Descriptor | Probable baseplate hub protein, Pore-forming tail tip protein pb2, Straight fiber protein pb4, ... (7 entities in total) |
| Functional Keywords | bacteriophage, siphophage, t5, baseplate, viral protein |
| Biological source | Escherichia phage T5 More |
| Total number of polymer chains | 36 |
| Total formula weight | 1664891.37 |
| Authors | Linares, R.,Arnaud, C.A.,Effantin, G.,Darnault, C.,Epalle, N.,Boeri Erba, E.,Schoehn, G.,Breyton, C. (deposition date: 2022-04-20, release date: 2023-02-08, Last modification date: 2023-07-05) |
| Primary citation | Linares, R.,Arnaud, C.A.,Effantin, G.,Darnault, C.,Epalle, N.H.,Boeri Erba, E.,Schoehn, G.,Breyton, C. Structural basis of bacteriophage T5 infection trigger and E. coli cell wall perforation. Sci Adv, 9:eade9674-eade9674, 2023 Cited by PubMed Abstract: Most bacteriophages present a tail allowing host recognition, cell wall perforation, and viral DNA channeling from the capsid to the infected bacterium cytoplasm. The majority of tailed phages bear a long flexible tail () at the tip of which receptor binding proteins (RBPs) specifically interact with their host, triggering infection. In siphophage T5, the unique RBP is located at the extremity of a central fiber. We present the structures of T5 tail tip, determined by cryo-electron microscopy before and after interaction with its receptor, FhuA, reconstituted into nanodisc. These structures bring out the important conformational changes undergone by T5 tail tip upon infection, which include bending of T5 central fiber on the side of the tail tip, tail anchoring to the membrane, tail tube opening, and formation of a transmembrane channel. The data allow to detail the first steps of an otherwise undescribed infection mechanism. PubMed: 36961893DOI: 10.1126/sciadv.ade9674 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.29 Å) |
Structure validation
Download full validation report
