Movie
Controller
Structure viewers
About EMN Papers
+Search query
-Structure paper
| Title | Double-stranded RNA virus outer shell assembly by bona fide domain-swapping. |
|---|---|
| Journal, issue, pages | Nat Commun, Vol. 8, Page 14814, Year 2017 |
| Publish date | Mar 13, 2017 |
 Authors | Zhaoyang Sun / Kamel El Omari / Xiaoyu Sun / Serban L Ilca / Abhay Kotecha / David I Stuart / Minna M Poranen / Juha T Huiskonen /   |
| PubMed Abstract | Correct outer protein shell assembly is a prerequisite for virion infectivity in many multi-shelled dsRNA viruses. In the prototypic dsRNA bacteriophage φ6, the assembly reaction is promoted by ...Correct outer protein shell assembly is a prerequisite for virion infectivity in many multi-shelled dsRNA viruses. In the prototypic dsRNA bacteriophage φ6, the assembly reaction is promoted by calcium ions but its biomechanics remain poorly understood. Here, we describe the near-atomic resolution structure of the φ6 double-shelled particle. The outer T=13 shell protein P8 consists of two alpha-helical domains joined by a linker, which allows the trimer to adopt either a closed or an open conformation. The trimers in an open conformation swap domains with each other. Our observations allow us to propose a mechanistic model for calcium concentration regulated outer shell assembly. Furthermore, the structure provides a prime exemplar of bona fide domain-swapping. This leads us to extend the theory of domain-swapping from the level of monomeric subunits and multimers to closed spherical shells, and to hypothesize a mechanism by which closed protein shells may arise in evolution. |
 External links | Nat Commun / PubMed:28287099 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.0 - 9.1 Å |
| Structure data | EMDB-3571, PDB-5muu: |
| Chemicals |  ChemComp-CA:  ChemComp-ADP: |
| Source |
|
 Keywords |  VIRUS / icosahedral virus capsid shell / HYDROLASE / packaging / ATPase / vertex / hyrdolase |
