Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7ZQP

Tail tip of siphophage T5 : open cone after interaction with bacterial receptor FhuA

Summary for 7ZQP
Entry DOI10.2210/pdb7zqp/pdb
EMDB information14873
DescriptorProbable baseplate hub protein, Probable tape measure protein (2 entities in total)
Functional Keywordsbacteriophage, siphophage, t5, baseplate, viral protein
Biological sourceEscherichia phage T5
More
Total number of polymer chains6
Total formula weight716758.03
Authors
Linares, R.,Arnaud, C.A.,Effantin, G.,Darnault, C.,Epalle, N.,Boeri Erba, E.,Schoehn, G.,Breyton, C. (deposition date: 2022-05-02, release date: 2023-02-08, Last modification date: 2023-07-05)
Primary citationLinares, 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: 36961893
DOI: 10.1126/sciadv.ade9674
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

227111

數據於2024-11-06公開中

PDB statisticsPDBj update infoContact PDBjnumon