7ZLV

Tail tip of siphophage T5 : central fibre protein pb4

Summary for 7ZLV

• Entry DOI: 10.2210/pdb7zlv/pdb
• EMDB information: 14790
• Descriptor: Probable central straight fiber (1 entity in total)
• Functional Keywords: bacteriophage, siphophage, t5, baseplate, viral protein, virus like particle
• Biological source: Escherichia phage T5 (Enterobacteria phage T5)
• Total number of polymer chains: 3
• Total formula weight: 224555.11

Authors

Linares, R.,Arnaud, C.A.,Effantin, G.,Epalle, N.,Boeri Erba, E.,Schoehn, G.,Breyton, C. (deposition date: 2022-04-15, release date: 2023-02-08, Last modification date: 2024-07-24)

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

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: 36961893
DOI: 10.1126/sciadv.ade9674

Experimental method

ELECTRON MICROSCOPY (4.22 Å)