8EGT
Capsid structure of Staphylococcus phage Andhra
Summary for 8EGT
| Entry DOI | 10.2210/pdb8egt/pdb |
| Related | 8EGR 8EGS |
| EMDB information | 28128 28129 28130 |
| Descriptor | gp19, capsid lining protein, Major capsid protein (2 entities in total) |
| Functional Keywords | phage capsid, hk97-like fold, virus |
| Biological source | Staphylococcus phage Andhra More |
| Total number of polymer chains | 8 |
| Total formula weight | 213978.95 |
| Authors | Hawkins, N.C.,Kizziah, J.L.,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 Cited by 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: 36449623DOI: 10.1126/sciadv.ade0459 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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