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| Title | The structure of gene product 6 of bacteriophage T4, the hinge-pin of the baseplate. |
|---|---|
| Journal, issue, pages | Structure, Vol. 17, Issue 6, Page 800-808, Year 2009 |
| Publish date | Jun 10, 2009 |
 Authors | Anastasia A Aksyuk / Petr G Leiman / Mikhail M Shneider / Vadim V Mesyanzhinov / Michael G Rossmann /  |
| PubMed Abstract | The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate ...The baseplate of bacteriophage T4 is a multicomponent protein complex, which controls phage attachment to the host. It assembles from six wedges and a central hub. During infection the baseplate undergoes a large conformational change from a dome-shaped to a flat, star-shaped structure. We report the crystal structure of the C-terminal half of gene product (gp) 6 and investigate its motion with respect to the other proteins during the baseplate rearrangement. Six gp6 dimers interdigitate, forming a ring that maintains the integrity of the baseplate in both conformations. One baseplate wedge contains an N-terminal dimer of gp6, whereas neighboring wedges are tied together through the C-terminal dimer of gp6. The dimeric interactions are preserved throughout the rearrangement of the baseplate. However, the hinge angle between the N- and C-terminal parts of gp6 changes by approximately 15 degrees , accounting for a 10 A radial increase in the diameter of the gp6 ring. |
 External links | Structure / PubMed:19523898 |
| Methods | X-ray diffraction / EM (single particle) |
| Resolution | 3.2 - 16 Å |
| Structure data |  PDB-3h2t:  PDB-3h3w:  PDB-3h3y: |
| Chemicals |  ChemComp-HOH: |
| Source |
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 Keywords | VIRAL PROTEIN / Virion / viral structural protein |
enterobacteria phage t4 (virus)