8EGR

Upper tail structure of Staphylococcus phage Andhra

Summary for 8EGR

• Entry DOI: 10.2210/pdb8egr/pdb
• Related: 8EGS 8EGT
• EMDB information: 28128 28129 28130
• Descriptor: gp15, receptor-binding protein, tail fiber, Upper collar protein, gp16, tail stem protein, ... (5 entities in total)
• Functional Keywords: phage tail, portal, receptor-binding protein, virus
• Biological source: Staphylococcus phage Andhra; More
• Total number of polymer chains: 24
• Total formula weight: 790478.51

Authors

Kizziah, J.L.,Hawkins, N.C.,Dokland, T. (deposition date: 2022-09-13, release date: 2022-12-14, Last modification date: 2024-06-19)

Primary citation

Hawkins, N.C.,Kizziah, J.L.,Hatoum-Aslan, A.,Dokland, T.
Structure and host specificity of Staphylococcus epidermidis bacteriophage Andhra.
Sci Adv, 8:eade0459-eade0459, 2022

PubMed Abstract: is an opportunistic pathogen of the human skin, often associated with infections of implanted medical devices. Staphylococcal picoviruses are a group of strictly lytic, short-tailed bacteriophages with compact genomes that are attractive candidates for therapeutic use. Here, we report the structure of the complete virion of -infecting phage Andhra, determined using high-resolution cryo-electron microscopy, allowing atomic modeling of 11 capsid and tail proteins. The capsid is a = 4 icosahedron containing a unique stabilizing capsid lining protein. The tail includes 12 trimers of a unique receptor binding protein (RBP), a lytic protein that also serves to anchor the RBPs to the tail stem, and a hexameric tail knob that acts as a gatekeeper for DNA ejection. Using structure prediction with AlphaFold, we identified the two proteins that comprise the tail tip heterooctamer. Our findings elucidate critical features for virion assembly, host recognition, and penetration.

PubMed: 36449623
DOI: 10.1126/sciadv.ade0459

Experimental method

ELECTRON MICROSCOPY (3.58 Å)