6V8I
Composite atomic model of the Staphylococcus aureus phage 80alpha baseplate
This is a non-PDB format compatible entry.
Summary for 6V8I
| Entry DOI | 10.2210/pdb6v8i/pdb |
| EMDB information | 20872 20873 20874 20875 20876 |
| Descriptor | Distal Tail Protein, gp58, Tail-Associated Lysin, gp59, Tape Measure Protein, gp57, ... (8 entities in total) |
| Functional Keywords | phage tail, tail tip, tape measure protein, viral protein |
| Biological source | Staphylococcus virus 80alpha More |
| Total number of polymer chains | 72 |
| Total formula weight | 4130159.81 |
| Authors | Kizziah, J.L.,Dokland, T. (deposition date: 2019-12-11, release date: 2020-03-04, Last modification date: 2024-03-06) |
| Primary citation | Kizziah, J.L.,Manning, K.A.,Dearborn, A.D.,Dokland, T. Structure of the host cell recognition and penetration machinery of a Staphylococcus aureus bacteriophage. Plos Pathog., 16:e1008314-e1008314, 2020 Cited by PubMed Abstract: Staphylococcus aureus is a common cause of infections in humans. The emergence of virulent, antibiotic-resistant strains of S. aureus is a significant public health concern. Most virulence and resistance factors in S. aureus are encoded by mobile genetic elements, and transduction by bacteriophages represents the main mechanism for horizontal gene transfer. The baseplate is a specialized structure at the tip of bacteriophage tails that plays key roles in host recognition, cell wall penetration, and DNA ejection. We have used high-resolution cryo-electron microscopy to determine the structure of the S. aureus bacteriophage 80α baseplate at 3.75 Å resolution, allowing atomic models to be built for most of the major tail and baseplate proteins, including two tail fibers, the receptor binding protein, and part of the tape measure protein. Our structure provides a structural basis for understanding host recognition, cell wall penetration and DNA ejection in viruses infecting Gram-positive bacteria. Comparison to other phages demonstrates the modular design of baseplate proteins, and the adaptations to the host that take place during the evolution of staphylococci and other pathogens. PubMed: 32069326DOI: 10.1371/journal.ppat.1008314 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.7 Å) |
Structure validation
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