8K39

Structure of the bacteriophage lambda portal vertex

This is a non-PDB format compatible entry.

Summary for 8K39

• Entry DOI: 10.2210/pdb8k39/pdb
• EMDB information: 36848
• Descriptor: Major capsid protein, Portal protein B (2 entities in total)
• Functional Keywords: complex, viral protein
• Biological source: Escherichia phage Lambda; More
• Total number of polymer chains: 42
• Total formula weight: 1861230.11

Authors

Xiao, H.,Tan, L.,Cheng, L.P.,Liu, H.R. (deposition date: 2023-07-14, release date: 2023-11-15, Last modification date: 2024-01-17)

Primary citation

Xiao, H.,Tan, L.,Tan, Z.,Zhang, Y.,Chen, W.,Li, X.,Song, J.,Cheng, L.,Liu, H.
Structure of the siphophage neck-Tail complex suggests that conserved tail tip proteins facilitate receptor binding and tail assembly.
Plos Biol., 21:e3002441-e3002441, 2023

PubMed Abstract: Siphophages have a long, flexible, and noncontractile tail that connects to the capsid through a neck. The phage tail is essential for host cell recognition and virus-host cell interactions; moreover, it serves as a channel for genome delivery during infection. However, the in situ high-resolution structure of the neck-tail complex of siphophages remains unknown. Here, we present the structure of the siphophage lambda "wild type," the most widely used, laboratory-adapted fiberless mutant. The neck-tail complex comprises a channel formed by stacked 12-fold and hexameric rings and a 3-fold symmetrical tip. The interactions among DNA and a total of 246 tail protein molecules forming the tail and neck have been characterized. Structural comparisons of the tail tips, the most diversified region across the lambda and other long-tailed phages or tail-like machines, suggest that their tail tip contains conserved domains, which facilitate tail assembly, receptor binding, cell adsorption, and DNA retaining/releasing. These domains are distributed in different tail tip proteins in different phages or tail-like machines. The side tail fibers are not required for the phage particle to orient itself vertically to the surface of the host cell during attachment.

PubMed: 38096144
DOI: 10.1371/journal.pbio.3002441

Experimental method

ELECTRON MICROSCOPY (4 Å)