5HX2
In vitro assembled star-shaped hubless T4 baseplate
Summary for 5HX2
| Entry DOI | 10.2210/pdb5hx2/pdb |
| EMDB information | 8064 |
| Descriptor | Baseplate wedge protein gp7, Baseplate wedge protein gp8, Baseplate wedge protein gp6, ... (5 entities in total) |
| Functional Keywords | t4, baseplate, complex, viral protein |
| Biological source | Enterobacteria phage T4 More |
| Total number of polymer chains | 9 |
| Total formula weight | 566241.06 |
| Authors | Yap, M.L.,Klose, T.,Fokine, A.,Rossmann, M.G. (deposition date: 2016-01-29, release date: 2016-03-02, Last modification date: 2024-03-06) |
| Primary citation | Yap, M.L.,Klose, T.,Arisaka, F.,Speir, J.A.,Veesler, D.,Fokine, A.,Rossmann, M.G. Role of bacteriophage T4 baseplate in regulating assembly and infection. Proc.Natl.Acad.Sci.USA, 113:2654-2659, 2016 Cited by PubMed Abstract: Bacteriophage T4 consists of a head for protecting its genome and a sheathed tail for inserting its genome into a host. The tail terminates with a multiprotein baseplate that changes its conformation from a "high-energy" dome-shaped to a "low-energy" star-shaped structure during infection. Although these two structures represent different minima in the total energy landscape of the baseplate assembly, as the dome-shaped structure readily changes to the star-shaped structure when the virus infects a host bacterium, the dome-shaped structure must have more energy than the star-shaped structure. Here we describe the electron microscopy structure of a 3.3-MDa in vitro-assembled star-shaped baseplate with a resolution of 3.8 Å. This structure, together with other genetic and structural data, shows why the high-energy baseplate is formed in the presence of the central hub and how the baseplate changes to the low-energy structure, via two steps during infection. Thus, the presence of the central hub is required to initiate the assembly of metastable, high-energy structures. If the high-energy structure is formed and stabilized faster than the low-energy structure, there will be insufficient components to assemble the low-energy structure. PubMed: 26929357DOI: 10.1073/pnas.1601654113 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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